Steven K. Chapman - Publications

Affiliations: 
Chemistry University of Edinburgh, Edinburgh, Scotland, United Kingdom 

144 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2012 Efimov I, Basran J, Sun X, Chauhan N, Chapman SK, Mowat CG, Raven EL. The mechanism of substrate inhibition in human indoleamine 2,3-dioxygenase. Journal of the American Chemical Society. 134: 3034-41. PMID 22299628 DOI: 10.1021/ja208694g  0.64
2010 Davydov RM, Chauhan N, Thackray SJ, Anderson JL, Papadopoulou ND, Mowat CG, Chapman SK, Raven EL, Hoffman BM. Probing the ternary complexes of indoleamine and tryptophan 2,3-dioxygenases by cryoreduction EPR and ENDOR spectroscopy. Journal of the American Chemical Society. 132: 5494-500. PMID 20353179 DOI: 10.1021/ja100518z  0.64
2010 Mowat CG, Gazur B, Campbell LP, Chapman SK. Flavin-containing heme enzymes. Archives of Biochemistry and Biophysics. 493: 37-52. PMID 19850002 DOI: 10.1016/j.abb.2009.10.005  0.64
2009 Chauhan N, Thackray SJ, Rafice SA, Eaton G, Lee M, Efimov I, Basran J, Jenkins PR, Mowat CG, Chapman SK, Raven EL. Reassessment of the reaction mechanism in the heme dioxygenases. Journal of the American Chemical Society. 131: 4186-7. PMID 19275153 DOI: 10.1021/ja808326g  0.64
2009 Pessanha M, Rothery EL, Miles CS, Reid GA, Chapman SK, Louro RO, Turner DL, Salgueiro CA, Xavier AV. Tuning of functional heme reduction potentials in Shewanella fumarate reductases Biochimica Et Biophysica Acta - Bioenergetics. 1787: 113-120. PMID 19081388 DOI: 10.1016/j.bbabio.2008.11.007  0.64
2008 Thackray SJ, Mowat CG, Chapman SK. Exploring the mechanism of tryptophan 2,3-dioxygenase. Biochemical Society Transactions. 36: 1120-3. PMID 19021508 DOI: 10.1042/BST0361120  0.64
2008 Paixão VB, Salgueiro CA, Brennan L, Reid GA, Chapman SK, Turner DL. The solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel family structural motif. Biochemistry. 47: 11973-80. PMID 18950243 DOI: 10.1021/bi801326j  0.64
2008 Li BR, Anderson JL, Mowat CG, Miles CS, Reid GA, Chapman SK. Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity. Biochemical Society Transactions. 36: 992-5. PMID 18793176 DOI: 10.1042/BST0360992  0.64
2008 Thackray SJ, Bruckmann C, Anderson JL, Campbell LP, Xiao R, Zhao L, Mowat CG, Forouhar F, Tong L, Chapman SK. Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding. Biochemistry. 47: 10677-84. PMID 18783250 DOI: 10.1021/bi801202a  0.64
2007 De Laurentis W, Khim L, Anderson JL, Adam A, Johnson KA, Phillips RS, Chapman SK, van Pee KH, Naismith JH. The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily. Biochemistry. 46: 12393-404. PMID 17924666 DOI: 10.1021/bi7012189  0.64
2007 Atkinson SJ, Mowat CG, Reid GA, Chapman SK. An octaheme c-type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine. Febs Letters. 581: 3805-8. PMID 17659281 DOI: 10.1016/j.febslet.2007.07.005  0.64
2007 Forouhar F, Anderson JL, Mowat CG, Vorobiev SM, Hussain A, Abashidze M, Bruckmann C, Thackray SJ, Seetharaman J, Tucker T, Xiao R, Ma LC, Zhao L, Acton TB, Montelione GT, ... Chapman SK, et al. Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America. 104: 473-8. PMID 17197414 DOI: 10.1073/pnas.0610007104  0.64
2007 De Laurentis W, Khim L, Ross Anderson JL, Adam A, Johnson KA, Phillips RS, Chapman SK, Van Pee KH, Naismith JH. The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily (Biochemistry (2007) 46, 43, (12393-12404)) Biochemistry. 46: 14733. DOI: 10.1021/bi702167m  0.64
2006 Celik A, Roberts GA, White JH, Chapman SK, Turner NJ, Flitsch SL. Probing the substrate specificity of the catalytically self-sufficient cytochrome P450 RhF from a Rhodococcus sp. Chemical Communications (Cambridge, England). 4492-4. PMID 17283795 DOI: 10.1039/b609427a  0.64
2006 Anderson JL, Chapman SK. Molecular mechanisms of enzyme-catalysed halogenation. Molecular Biosystems. 2: 350-7. PMID 16880954 DOI: 10.1039/b607813c  0.64
2006 Gibson HR, Mowat CG, Miles CS, Li BR, Leys D, Reid GA, Chapman SK. Structural and functional studies on DHC, the diheme cytochrome c from Rhodobacter sphaeroides, and its interaction with SHP, the sphaeroides heme protein. Biochemistry. 45: 6363-71. PMID 16700547 DOI: 10.1021/bi060288q  0.64
2006 Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK. A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. The Journal of Biological Chemistry. 281: 20589-97. PMID 16699170 DOI: 10.1074/jbc.M603077200  0.64
2006 Wardrope C, Mowat CG, Walkinshaw MD, Reid GA, Chapman SK. Fumarate reductase: structural and mechanistic insights from the catalytic reduction of 2-methylfumarate. Febs Letters. 580: 1677-80. PMID 16497301 DOI: 10.1016/j.febslet.2006.02.016  0.64
2006 Clark JP, Miles CS, Mowat CG, Walkinshaw MD, Reid GA, Daff SN, Chapman SK. The role of Thr268 and Phe393 in cytochrome P450 BM3. Journal of Inorganic Biochemistry. 100: 1075-90. PMID 16403573 DOI: 10.1016/j.jinorgbio.2005.11.020  0.64
2005 Mowat CG, Chapman SK. Multi-heme cytochromes--new structures, new chemistry. Dalton Transactions (Cambridge, England : 2003). 3381-9. PMID 16234915 DOI: 10.1039/b505184c  0.64
2005 Hunter DJ, Roberts GA, Ost TW, White JH, Müller S, Turner NJ, Flitsch SL, Chapman SK. Analysis of the domain properties of the novel cytochrome P450 RhF. Febs Letters. 579: 2215-20. PMID 15811344 DOI: 10.1016/j.febslet.2005.03.016  0.64
2005 Anderson JL, Chapman SK. Ligand probes for heme proteins. Dalton Transactions (Cambridge, England : 2003). 13-24. PMID 15605142 DOI: 10.1039/b413046d  0.64
2004 Pessanha M, Rothery EL, Louro RO, Turner DL, Miles CS, Reid GA, Chapman SK, Xavier AV, Salgueiro CA. Redox behaviour of the haem domain of flavocytochrome c 3 from Shewanella frigidimarina probed by NMR Febs Letters. 578: 185-190. PMID 15581639 DOI: 10.1016/j.febslet.2004.10.098  0.64
2004 Ost TW, Clark JP, Anderson JL, Yellowlees LJ, Daff S, Chapman SK. 4-cyanopyridine, a versatile spectroscopic probe for cytochrome P450 BM3. The Journal of Biological Chemistry. 279: 48876-82. PMID 15364917 DOI: 10.1074/jbc.M408601200  0.64
2004 Mowat CG, Rothery E, Miles CS, McIver L, Doherty MK, Drewette K, Taylor P, Walkinshaw MD, Chapman SK, Reid GA. Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nature Structural & Molecular Biology. 11: 1023-4. PMID 15361860 DOI: 10.1038/nsmb827  0.64
2004 Mowat CG, Wehenkel A, Green AJ, Walkinshaw MD, Reid GA, Chapman SK. Altered substrate specificity in flavocytochrome b2: structural insights into the mechanism of L-lactate dehydrogenation. Biochemistry. 43: 9519-26. PMID 15260495 DOI: 10.1021/bi049263m  0.64
2004 Gustafsson MC, Roitel O, Marshall KR, Noble MA, Chapman SK, Pessegueiro A, Fulco AJ, Cheesman MR, von Wachenfeldt C, Munro AW. Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium. Biochemistry. 43: 5474-87. PMID 15122913 DOI: 10.1021/bi035904m  0.64
2004 Rothery EL, Mowat CG, Miles CS, Mott S, Walkinshaw MD, Reid GA, Chapman SK. Probing domain mobility in a flavocytochrome. Biochemistry. 43: 4983-9. PMID 15109257 DOI: 10.1021/bi030261w  0.64
2003 Ost TW, Clark J, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK, Daff S. Oxygen activation and electron transfer in flavocytochrome P450 BM3. Journal of the American Chemical Society. 125: 15010-20. PMID 14653735 DOI: 10.1021/ja035731o  0.64
2003 Rothery EL, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK. Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina. Biochemistry. 42: 13160-9. PMID 14609326 DOI: 10.1021/bi030159z  0.64
2003 Roberts GA, Celik A, Hunter DJ, Ost TW, White JH, Chapman SK, Turner NJ, Flitsch SL. A self-sufficient cytochrome p450 with a primary structural organization that includes a flavin domain and a [2Fe-2S] redox center. The Journal of Biological Chemistry. 278: 48914-20. PMID 14514666 DOI: 10.1074/jbc.M309630200  0.64
2003 Schwalb C, Chapman SK, Reid GA. The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis. Biochemistry. 42: 9491-7. PMID 12899636 DOI: 10.1021/bi034456f  0.64
2003 Fullerton SW, Daff S, Sanders DA, Ingledew WJ, Whitfield C, Chapman SK, Naismith JH. Potentiometric analysis of UDP-galactopyranose mutase: stabilization of the flavosemiquinone by substrate. Biochemistry. 42: 2104-9. PMID 12590598 DOI: 10.1021/bi027077f  0.64
2003 Green AJ, Munro AW, Cheesman MR, Reid GA, von Wachenfeldt C, Chapman SK. Expression, purification and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 BioI. Journal of Inorganic Biochemistry. 93: 92-9. PMID 12538057 DOI: 10.1016/S0162-0134(02)00456-7  0.64
2003 Leys D, Mowat CG, McLean KJ, Richmond A, Chapman SK, Walkinshaw MD, Munro AW. Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450. The Journal of Biological Chemistry. 278: 5141-7. PMID 12435731 DOI: 10.1074/jbc.M209928200  0.64
2003 Pessanha M, Louro RO, Correia IJ, Rothery EL, Pankhurst KL, Reid GA, Chapman SK, Turner DL, Salgueiro CA. Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3. The Biochemical Journal. 370: 489-95. PMID 12413396 DOI: 10.1042/BJ20021408  0.64
2003 Pessanha M, Turner DL, Rothery EL, Pankhurst KL, Reid GA, Chapman SK, Xavier AV, Salgueiro CA. NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina Inorganica Chimica Acta. 356: 379-381. DOI: 10.1016/S0020-1693(03)00179-8  0.64
2002 Louro RO, Pessanha M, Reid GA, Chapman SK, Turner DL, Salgueiro CA. Determination of the orientation of the axial ligands and of the magnetic properties of the haems in the tetrahaem ferricytochrome from Shewanella frigidimarina. Febs Letters. 531: 520-4. PMID 12435604 DOI: 10.1016/S0014-5793(02)03610-4  0.64
2002 Mowat CG, Pankhurst KL, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK. Engineering water to act as an active site acid catalyst in a soluble fumarate reductase. Biochemistry. 41: 11990-6. PMID 12356299 DOI: 10.1021/bi0203177  0.64
2002 McLean KJ, Cheesman MR, Rivers SL, Richmond A, Leys D, Chapman SK, Reid GA, Price NC, Kelly SM, Clarkson J, Smith WE, Munro AW. Expression, purification and spectroscopic characterization of the cytochrome P450 CYP121 from Mycobacterium tuberculosis. Journal of Inorganic Biochemistry. 91: 527-41. PMID 12237220 DOI: 10.1016/S0162-0134(02)00479-8  0.64
2002 Fuziwara S, Sagami I, Rozhkova E, Craig D, Noble MA, Munro AW, Chapman SK, Shimizu T. Catalytically functional flavocytochrome chimeras of P450 BM3 and nitric oxide synthase. Journal of Inorganic Biochemistry. 91: 515-26. PMID 12237219 DOI: 10.1016/S0162-0134(02)00478-6  0.64
2002 Schwalb C, Chapman SK, Reid GA. The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella. Biochemical Society Transactions. 30: 658-62. PMID 12196158 DOI: 10.1042/  0.64
2002 Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK. Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina. Biochemistry. 41: 8551-6. PMID 12093271 DOI: 10.1021/bi020155e  0.64
2002 Craig DH, Chapman SK, Daff S. Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock. The Journal of Biological Chemistry. 277: 33987-94. PMID 12089147 DOI: 10.1074/jbc.M203118200  0.64
2002 Munro AW, Leys DG, McLean KJ, Marshall KR, Ost TW, Daff S, Miles CS, Chapman SK, Lysek DA, Moser CC, Page CC, Dutton PL. P450 BM3: the very model of a modern flavocytochrome. Trends in Biochemical Sciences. 27: 250-7. PMID 12076537 DOI: 10.1016/S0968-0004(02)02086-8  0.64
2002 Jeuken LJ, Jones AK, Chapman SK, Cecchini G, Armstrong FA. Electron-transfer mechanisms through biological redox chains in multicenter enzymes. Journal of the American Chemical Society. 124: 5702-13. PMID 12010043 DOI: 10.1021/ja012638w  0.64
2002 Mowat CG, Leys D, McLean KJ, Rivers SL, Richmond A, Munro AW, Ortiz Lombardia M, Alzari PM, Reid GA, Chapman SK, Walkinshaw MD. Crystallization and preliminary crystallographic analysis of a novel cytochrome P450 from Mycobacterium tuberculosis. Acta Crystallographica. Section D, Biological Crystallography. 58: 704-5. PMID 11914502 DOI: 10.1107/S0907444902002676  0.64
2002 Cunane LM, Barton JD, Chen ZW, Welsh FE, Chapman SK, Reid GA, Mathews FS. Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme. Biochemistry. 41: 4264-72. PMID 11914072 DOI: 10.1021/bi0119870  0.64
2001 Ost TW, Munro AW, Mowat CG, Taylor PR, Pesseguiero A, Fulco AJ, Cho AK, Cheesman MA, Walkinshaw MD, Chapman SK. Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3. Biochemistry. 40: 13430-8. PMID 11695889 DOI: 10.1021/bi010717e  0.64
2001 Ost TW, Miles CS, Munro AW, Murdoch J, Reid GA, Chapman SK. Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3. Biochemistry. 40: 13421-9. PMID 11695888 DOI: 10.1021/bi010716m  0.64
2001 Mowat CG, Moysey R, Miles CS, Leys D, Doherty MK, Taylor P, Walkinshaw MD, Reid GA, Chapman SK. Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase. Biochemistry. 40: 12292-8. PMID 11591148 DOI: 10.1021/bi011360h  0.64
2001 Craig DH, Barna T, Moody PC, Bruce NC, Chapman SK, Munro AW, Scrutton NS. Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N-1 atom and C-2 carbonyl region of the active-site flavin. The Biochemical Journal. 359: 315-23. PMID 11583577 DOI: 10.1042/0264-6021:3590315  0.64
2001 Green AJ, Rivers SL, Cheeseman M, Reid GA, Quaroni LG, Macdonald ID, Chapman SK, Munro AW. Expression, purification and characterization of cytochrome P450 Biol: a novel P450 involved in biotin synthesis in Bacillus subtilis. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 523-33. PMID 11472016 DOI: 10.1007/s007750100229  0.64
2001 Daff S, Noble MA, Craig DH, Rivers SL, Chapman SK, Munro AW, Fujiwara S, Rozhkova E, Sagami I, Shimizu T. Control of electron transfer in neuronal NO synthase. Biochemical Society Transactions. 29: 147-52. PMID 11356143 DOI: 10.1042/0300-5127:0290147  0.64
2001 Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK. Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry. 40: 1956-63. PMID 11329262 DOI: 10.1021/bi001718u  0.64
2001 Talfournier F, Munro AW, Basran J, Sutcliffe MJ, Daff S, Chapman SK, Scrutton NS. alpha Arg-237 in Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein affords approximately 200-millivolt stabilization of the FAD anionic semiquinone and a kinetic block on full reduction to the dihydroquinone. The Journal of Biological Chemistry. 276: 20190-6. PMID 11285259 DOI: 10.1074/jbc.M010853200  0.64
2001 Pessanha M, Brennan L, Xavier AV, Cuthbertson PM, Reid GA, Chapman SK, Turner DL, Salgueiro CA. NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: Identification of the haem-specific axial ligands and order of oxidation Febs Letters. 489: 8-13. PMID 11231004 DOI: 10.1016/S0014-5793(00)02383-8  0.64
2001 Liu H, Hill HAO, Chapman SK. Electrochemistry of the flavodehydrogenase domain of flavocytochrome b2 engineered for L-mandelate dehydrogenase activity Journal of Electroanalytical Chemistry. 500: 598-603. DOI: 10.1016/S0022-0728(00)00440-X  0.64
2001 Liu H, Hill HAO, Chapman SK. Electrochemical property of L-mandalate dehydrogenase Fenxi Huaxue. 29: 758-759.  0.64
2000 Munro AW, Noble MA, Ost TW, Green AJ, McLean KJ, Robledo L, Miles CS, Murdoch J, Chapman SK. Flavocytochrome P450 BM3 substrate selectivity and electron transfer in a model cytochrome P450. Sub-Cellular Biochemistry. 35: 297-315. PMID 11192726  0.64
2000 Mowat CG, Chapman SK. Flavocytochrome b2. Sub-Cellular Biochemistry. 35: 279-95. PMID 11192724  0.64
2000 Miles CS, Ost TW, Noble MA, Munro AW, Chapman SK. Protein engineering of cytochromes P-450. Biochimica Et Biophysica Acta. 1543: 383-407. PMID 11150615 DOI: 10.1016/S0167-4838(00)00236-3  0.64
2000 Ost TW, Miles CS, Murdoch J, Cheung Y, Reid GA, Chapman SK, Munro AW. Rational re-design of the substrate binding site of flavocytochrome P450 BM3. Febs Letters. 486: 173-7. PMID 11113461 DOI: 10.1016/S0014-5793(00)02267-5  0.64
2000 Leadbeater C, McIver L, Campopiano DJ, Webster SP, Baxter RL, Kelly SM, Price NC, Lysek DA, Noble MA, Chapman SK, Munro AW. Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase. The Biochemical Journal. 352: 257-66. PMID 11085917 DOI: 10.1042/0264-6021:3520257  0.64
2000 Mowat CG, Miles CS, Munro AW, Cheesman MR, Quaroni LG, Reid GA, Chapman SK. Changing the heme ligation in flavocytochrome b2: substitution of histidine-66 by cysteine. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 584-92. PMID 11085649 DOI: 10.1007/s007750000141  0.64
2000 Reid GA, Miles CS, Moysey RK, Pankhurst KL, Chapman SK. Catalysis in fumarate reductase. Biochimica Et Biophysica Acta. 1459: 310-5. PMID 11004445 DOI: 10.1016/S0005-2728(00)00166-3  0.64
2000 Doherty MK, Pealing SL, Miles CS, Moysey R, Taylor P, Walkinshaw MD, Reid GA, Chapman SK. Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study. Biochemistry. 39: 10695-701. PMID 10978153 DOI: 10.1021/bi000871l  0.64
2000 Gordon EH, Pike AD, Hill AE, Cuthbertson PM, Chapman SK, Reid GA. Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration. The Biochemical Journal. 349: 153-8. PMID 10861223 DOI: 10.1042/0264-6021:3490153  0.64
2000 Koppenhöfer A, Turner KL, Allen JW, Chapman SK, Ferguson SJ. Cytochrome cd(1) from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior. Biochemistry. 39: 4243-9. PMID 10757972 DOI: 10.1021/bi000192a  0.64
2000 Mowat CG, Beaudoin I, Durley RC, Barton JD, Pike AD, Chen ZW, Reid GA, Chapman SK, Mathews FS, Lederer F. Kinetic and crystallographic studies on the active site Arg289Lys mutant of flavocytochrome b2 (yeast L-lactate dehydrogenase). Biochemistry. 39: 3266-75. PMID 10727218 DOI: 10.1021/bi9925975  0.64
2000 Jones AK, Camba R, Reid GA, Chapman SK, Armstrong FA. Interruption and time-resolution of catalysis by a flavoenzyme using fast scan protein film voltammetry [4] Journal of the American Chemical Society. 122: 6494-6495. DOI: 10.1021/ja000848n  0.64
1999 Noble MA, Munro AW, Rivers SL, Robledo L, Daff SN, Yellowlees LJ, Shimizu T, Sagami I, Guillemette JG, Chapman SK. Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase. Biochemistry. 38: 16413-8. PMID 10600101 DOI: 10.1021/bi992150w  0.64
1999 Taylor P, Pealing SL, Reid GA, Chapman SK, Walkinshaw MD. Structural and mechanistic mapping of a unique fumarate reductase. Nature Structural Biology. 6: 1108-12. PMID 10581550 DOI: 10.1038/70045  0.64
1999 Sharp RE, Chapman SK. Mechanisms for regulating electron transfer in multi-centre redox proteins. Biochimica Et Biophysica Acta. 1432: 143-58. PMID 10407138 DOI: 10.1016/S0167-4838(99)00109-0  0.64
1999 Noble MA, Miles CS, Chapman SK, Lysek DA, MacKay AC, Reid GA, Hanzlik RP, Munro AW. Roles of key active-site residues in flavocytochrome P450 BM3. The Biochemical Journal. 339: 371-9. PMID 10191269 DOI: 10.1042/0264-6021:3390371  0.64
1999 Munro AW, Noble MA, Miles CS, Daff SN, Green AJ, Quaroni L, Rivers S, Ost TW, Reid GA, Chapman SK. Flavocytochrome P-450 BM3: a paradigm for the analysis of electron transfer and its control in the P-450s. Biochemical Society Transactions. 27: 190-6. PMID 10093732  0.64
1999 Chapman SK, Welsh F, Moysey R, Mowat C, Doherty MK, Turner KL, Munro AW, Reid GA. Flavocytochromes: transceivers and relays in biological electron transfer. Biochemical Society Transactions. 27: 185-9. PMID 10093731  0.64
1999 Turner KL, Doherty MK, Heering HA, Armstrong FA, Reid GA, Chapman SK. Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400. Biochemistry. 38: 3302-9. PMID 10079073 DOI: 10.1021/bi9826308  0.64
1998 Noble MA, Quaroni L, Chumanov GD, Turner KL, Chapman SK, Hanzlik RP, Munro AW. Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3. Biochemistry. 37: 15799-807. PMID 9843385 DOI: 10.1021/bi980462d  0.64
1998 McIver L, Leadbeater C, Campopiano DJ, Baxter RL, Daff SN, Chapman SK, Munro AW. Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli. European Journal of Biochemistry / Febs. 257: 577-85. PMID 9839946  0.64
1998 Noble MA, Turner KL, Chapman SK, Munro AW. Mechanistic probes of flavocytochrome P-450 BM3. Biochemical Society Transactions. 26: S213. PMID 9765932  0.64
1998 Munro AW, Noble MA, Turner KL, Chapman SK. The interaction of eukaryotic cytochrome b5 with flavocytochrome P-450 BM3 from Bacillus megaterium. Biochemical Society Transactions. 26: S212. PMID 9765931  0.64
1998 Reid GA, Gordon EH, Hill AE, Doherty M, Turner K, Holt R, Chapman SK. Structure and function of flavocytochrome c3, the soluble fumarate reductase from Shewanella NCIMB400. Biochemical Society Transactions. 26: 418-21. PMID 9765890  0.64
1998 Sinclair R, Reid GA, Chapman SK. Re-design of Saccharomyces cerevisiae flavocytochrome b2: introduction of L-mandelate dehydrogenase activity. The Biochemical Journal. 333: 117-20. PMID 9639570  0.64
1998 Illias RM, Sinclair R, Robertson D, Neu A, Chapman SK, Reid GA. L-Mandelate dehydrogenase from Rhodotorula graminis: cloning, sequencing and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain. The Biochemical Journal. 333: 107-15. PMID 9639569  0.64
1998 Gordon EH, Pealing SL, Chapman SK, Ward FB, Reid GA. Physiological function and regulation of flavocytochrome c3, the soluble fumarate reductase from Shewanella putrefaciens NCIMB 400. Microbiology (Reading, England). 144: 937-45. PMID 9579067 DOI: 10.1099/00221287-144-4-937  0.64
1998 Short DM, Walkinshaw MD, Taylor P, Reid GA, Chapman SK. Location of a cytochrome c binding site on the surface of flavocytochrome b2 Journal of Biological Inorganic Chemistry. 3: 246-252. DOI: 10.1007/s007750050228  0.64
1997 Munro AW, Daff SN, Turner KL, Chapman SK. Probing inter-domain electron transfer in a model flavocytochrome P-450. Biochemical Society Transactions. 25: S629. PMID 9450057  0.64
1997 Munro AW, Daff SN, Turner KL, Chapman SK. Redox characterisation of flavocytochrome P-450 BM3 from Bacillus megaterium. Biochemical Society Transactions. 25: S628. PMID 9450056  0.64
1997 Daff SN, Chapman SK, Turner KL, Holt RA, Govindaraj S, Poulos TL, Munro AW. Redox control of the catalytic cycle of flavocytochrome P-450 BM3. Biochemistry. 36: 13816-23. PMID 9374858 DOI: 10.1021/bi971085s  0.64
1997 Munro AW, Daff SN, Turver K, Chapman SK. Redox control of catnlys.s in flavixytochrome P-450 BM3 Faseb Journal. 11.  0.64
1997 Munro AW, Daff SN, Turner KL, Chapman SK. 95 Probing inter-domain electron transfer in a model flavocytochrome P-450 Biochemical Society Transactions. 25.  0.64
1997 Munro AW, Daff SN, Turner KL, Chapman SK. 94 Redox characterisation of flavocytochrome P-450 BM3 from Bacillus megaterium Biochemical Society Transactions. 25.  0.64
1997 Jacob C, Safronov AY, Wilson S, Hill HAO, Booth TF, Chapman SK. Redox-active lipid-incorporating proteins as a novel immobilisation technique Journal of Electroanalytical Chemistry. 430: 119-125.  0.64
1996 Munro AW, Daff S, Coggins JR, Lindsay JG, Chapman SK. Probing electron transfer in flavocytochrome P-450 BM3 and its component domains. European Journal of Biochemistry / Febs. 239: 403-9. PMID 8706747  0.64
1996 Sharp RE, Chapman SK, Reid GA. Modulation of flavocytochrome b2 intraprotein electron transfer via an interdomain hinge region. The Biochemical Journal. 316: 507-13. PMID 8687394  0.64
1996 Chapman SK, Reid GA, Bell C, Short D, Daff S. Flavocytochrome b2: an ideal model system for studying protein-mediated electron transfer. Biochemical Society Transactions. 24: 73-7. PMID 8674751 DOI: 10.1016/S0898-8838(08)60041-0  0.64
1996 Munro AW, Coggins JR, Lindsay JG, Daff S, Chapman SK. Formation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH. Biochemical Society Transactions. 24: 18S. PMID 8674656  0.64
1996 Daff S, Sharp RE, Short DM, Bell C, White P, Manson FDC, Reid GA, Chapman SK. Interaction of cytochrome c with flavocytochrome b2 Biochemistry. 35: 6351-6357. PMID 8639580 DOI: 10.1021/bi9522561  0.64
1996 Daff S, Ingledew WJ, Reid GA, Chapman SK. New insights into the catalytic cycle of flavocytochrome b2. Biochemistry. 35: 6345-50. PMID 8639579 DOI: 10.1021/bi9522559  0.64
1996 Sharp RE, Chapman SK, Reid GA. Deletions in the interdomain hinge region of flavocytochrome b2: effects on intraprotein electron transfer. Biochemistry. 35: 891-9. PMID 8547270 DOI: 10.1021/bi950457z  0.64
1996 Sharp RE, Chapman SK, Reid GA. Modulation of flavocytochrome b2 intraprotein electron transfer via an interdomain hinge region Biochemical Journal. 316: 507-513.  0.64
1995 Gaume B, Sharp RE, Manson FDC, Chapman SK, Reid GA, Lederer F. Mutation to glutamine of histidine 373, the catalytic base of flavocytochrome b2 (L-lactate dehydrogenase) Biochimie. 77: 621-630. PMID 8589072 DOI: 10.1016/0300-9084(96)88177-6  0.64
1995 Gondry M, Diêp Lê KH, Manson FD, Chapman SK, Mathews FS, Reid GA, Lederer F. On the lack of coordination between protein folding and flavin insertion in Escherichia coli for flavocytochrome b2 mutant forms Y254L and D282N. Protein Science : a Publication of the Protein Society. 4: 925-35. PMID 7663348 DOI: 10.1002/pro.5560040512  0.64
1995 Balme A, Brunt CE, Pallister RL, Chapman SK, Reid GA. Isolation and characterization of the flavin-binding domain of flavocytochrome b2 expressed independently in Escherichia coli. The Biochemical Journal. 309: 601-5. PMID 7626026  0.64
1995 Chapman SK, Mount AR. Electron transfer in proteins Natural Product Reports. 12: 93-100.  0.64
1994 Sharp RE, White P, Chapman SK, Reid GA. Role of the interdomain hinge of flavocytochrome b2 in intra- and inter-protein electron transfer Biochemistry. 33: 5115-5120. PMID 8172886  0.64
1994 Smekal O, Reid GA, Chapman SK. Substrate analogues as probes of the catalytic mechanism of L-mandelate dehydrogenase from Rhodoforula graminis Biochemical Journal. 297: 647-652. PMID 8110205  0.64
1994 Morris CJ, Black AC, Pealing SL, Manson FDC, Chapman SK, Reid GA, Gibson DM, Ward FB. Purification and properties of a novel cytochrome: Flavocytochrome c from Shewanella putrefaciens Biochemical Journal. 302: 587-593. PMID 8093012  0.64
1994 Daff S, Manson FDC, Reid GA, Chapman SK. Strategic manipulation of the substrate specificity of Saccharomyces cerevisiae flavocytochrome b2 Biochemical Journal. 301: 829-834. PMID 8053908  0.64
1994 Chapman SK, Reid GA, Daff S, Sharp RE, White P, Manson FDC, Lederer F. Flavin to haem electron transfer in flavocytochrome b2 Biochemical Society Transactions. 22: 713-718. PMID 7821670  0.64
1994 Daff S, Manson FDC, Reid GA, Chapman SK. Manipulation of the substrate specificity of flavocytochrome b2 Biochemical Society Transactions. 22: 282S. PMID 7821541  0.64
1994 Sharp RE, White P, Chapman SK, Reid GA. The use of deletion mutants in the hinge region as functional probes of flavocytochromc b2 Biochemical Society Transactions. 22: 281S. PMID 7821540  0.64
1994 McFarlane J, Taylor P, Pealing SL, Chapman SK, Reid GA. Flavocytochrome b2: Probing domain mobility by introducing disulphide bridges Biochemical Society Transactions. 22: 280S. PMID 7821539  0.64
1994 White P, Short DM, Manson FDC, Chapman SK, Reid GA. Investigation of interdomain communication in flavocytochrome b2 by generation of interspecies hybrid enzymes Biochemical Society Transactions. 22: 279S. PMID 7821538  0.64
1994 Lloyd E, Chapman K, Chapman SK, Jia ZS, Lim MC, Tomkinson NP, Salmon GA, Sykes AG. Rate constants for intramolecular electron-transfer reactions of ruthenium-modified histidine mutants of cytochrome b2 Journal of the Chemical Society, Dalton Transactions. 675-681. DOI: 10.1039/DT9940000675  0.64
1993 Smekal O, Yasin M, Fewson CA, Reid GA, Chapman SK. L-Mandelate dehydrogenase from Rhodotorula graminis: Comparisons with the L-lactate dehydrogenase (flavocytochrome b2) from Saccharomyces cerevisiae Biochemical Journal. 290: 103-107. PMID 8439280  0.64
1993 Miles CS, Manson FDC, Reid GA, Chapman SK. Substitution of a haem-iron axial ligand in flavocytochrome b2 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1202: 82-86. PMID 8396977 DOI: 10.1016/0167-4838(93)90066-Z  0.64
1993 White P, Manson FDC, Brunt CE, Chapman SK, Reid GA. The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b2 Biochemical Journal. 291: 89-94. PMID 8385941  0.64
1992 Miles CS, Rouviere-Fourmy N, Lederer F, Mathews FS, Reid GA, Black MT, Chapman SK. Tyr-143 facilitates interdomain electron transfer in flavocytochrome b2 Biochemical Journal. 285: 187-192. PMID 1637299  0.64
1992 Brunt CE, Cox MC, Thurgood AG, Moore GR, Reid GA, Chapman SK. Isolation and characterization of the cytochrome domain of flavocytochrome b2 expressed independently in Escherichia coli. The Biochemical Journal. 283: 87-90. PMID 1567382  0.64
1992 Pealing SL, Black AC, Manson FDC, Ward FB, Chapman SK, Reid GA. Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: A tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria Biochemistry. 31: 12132-12140. PMID 1333793  0.64
1990 Wallis MG, Chapman SK. Isolation and partial characterization of an extradiol non-haem iron dioxygenase which preferentially cleaves 3-methylcatechol Biochemical Journal. 266: 605-609. PMID 2317207  0.64
1990 Dubois J, Chapman SK, Mathews FS, Reid GA, Lederer F. Substitution of Tyr254 with Phe at the active site of flavocytochrome b2: Consequences on catalysis of lactate dehydrogenation Biochemistry. 29: 6393-6400. PMID 2207080  0.64
1989 Black MT, Gunn FJ, Chapman SK, Reid GA. Structural basis for the kinetic differences between flavocytochromes b2 from the yeasts Hansenula anomala and Saccharomyces cerevisiae Biochemical Journal. 263: 973-976. PMID 2688640  0.64
1989 White SA, Black MT, Reid GA, Chapman SK. The role of the C-terminal tail of flavocytochrome b2 Biochemical Journal. 263: 849-853. PMID 2688637  0.64
1989 McLean PA, Wink DA, Chapman SK, Hickman AB, McKillop DM, Orme-Johnson WH. A new method for extraction of iron-molybdenum cofactor (FeMoco) from nitrogenase adsorbed to DEAE-cellulose. 1. Effects of anions, cations, and preextraction treatments. Biochemistry. 28: 9402-6. PMID 2611239  0.64
1988 Reid GA, White S, Black MT, Lederer F, Mathews FS, Chapman SK. Probing the active site of flavocytochrome b2 by site-directed mutagenesis European Journal of Biochemistry. 178: 329-333. PMID 3061813 DOI: 10.1111/j.1432-1033.1988.tb14454.x  0.64
1986 Armstrong GD, Chapman SK, Sisley MJ, Sykes AG, Aitken A, Osheroff N, Margoliash E. Preferred sites on cytochrome c for electron transfer with two positively charged blue copper proteins, Anabaena variabilis plastocyanin and stellacyanin. Biochemistry. 25: 6947-51. PMID 3026438  0.64
1986 Chapman SK, Orme-Johnson WH, McGinnis J, Sinclair-Day JD, Sykes AG, Ohlsson PI, Paul KG. Kinetic, spectroscopic, and structural (extended X-ray absorption fine structure) studies on the type 1 blue copper protein umecyanin Journal of the Chemical Society, Dalton Transactions. 2063-2068. DOI: 10.1039/DT9860002063  0.64
1986 Walters MA, Chapman SK, Orme-Johnson WH. The nature of amide ligation to the metal sites of FeMoco Polyhedron. 5: 561-565. DOI: 10.1016/S0277-5387(00)84964-5  0.64
1985 Beoku-Betts D, Chapman SK, Knox CV, Sykes AG. Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. 11. Effects of pH, competitive inhibition, and chromium(III) modification on the reaction of plastocyanin with cytochrome f Inorganic Chemistry. 24: 1677-1681.  0.64
1984 Chapman SK, Knox CV, Sykes AG. Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. Part 10. The assignment of binding sites in the reactions of plastocyanin (and azurin) with non-physiological protein redox partners Journal of the Chemical Society, Dalton Transactions. 2775-2780. DOI: 10.1039/DT9840002775  0.64
1984 Chapman SK, Knox CV, Kathirgamanathan P, Sykes AG. Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. Part 9. Effects of chromium(III) modification on reactions of plastocyanin with [Co(phen)3]3+ (phen = 1,10-phenanthroline), [Fe(CN)6]3-.. Journal of the Chemical Society, Dalton Transactions. 2769-2773. DOI: 10.1039/DT9840002769  0.64
1984 Augustin MA, Chapman SK, Davies DM, Watson AD, Sykes AG. Kinetic studies on 1:1 electron transfer reactions involving blue copper proteins. 8. Reactions of plastocyanin and azurin with cytochrome c and high potential iron-sulfur protein Journal of Inorganic Biochemistry. 20: 281-289. DOI: 10.1016/0162-0134(84)85027-8  0.64
1984 Chapman SK, Davies DM, Vuik CPJ, Sykes AG. Kinetic studies on the oxidation of calf liver cytochrome b5 with inorganic complexes Journal of the American Chemical Society. 106: 2692-2696.  0.64
1983 Augustin MA, Chapman SK, Davies DM, Sykes AG, Speck SH, Margoliash E. Interaction of cytochrome c with the blue copper proteins, plastocyanin and azurin. The Journal of Biological Chemistry. 258: 6405-9. PMID 6304038  0.64
1983 Butler J, Chapman SK, Davies DM, Sykes AG, Speck SH, Osheroff N, Margoliash E. Preferred sites for electron transfer between cytochrome c and iron and cobalt complexes. The Journal of Biological Chemistry. 258: 6400-4. PMID 6304037  0.64
1983 Chapman SK, Sanemasa I, Sykes AG. Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. Part 7. Effects of pH and redox-inactive [Pt(NH<inf>3</inf>)<inf>6</inf>]<sup>4+</sup> on reactions of parsley plastocyanin with different inorganic redox partners Journal of the Chemical Society, Dalton Transactions. 2549-2553. DOI: 10.1039/DT9830002549  0.64
1983 Chapman SK, Watson AD, Sykes AG. Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. Part 6. Competitive inhibition of the [Co(phen)<inf>3</inf>]<sup>3+</sup> (phen = 1,10-phenanthroline) oxidation of parsley plastocyanin PCu(I) by redox-inactive complexes Journal of the Chemical Society, Dalton Transactions. 2543-2548. DOI: 10.1039/DT9830002543  0.64
1983 Chapman SK, Sanemasa I, Watson AD, Sykes AG. Kinetic studies on 1: 1 electron-transfer reactions involving blue copper proteins. Part 5. Reactions of parsley plastocyanin and Pseudomonas aeruginosa azurin with the negatively charged oxidants [(NC)<inf>5</inf>FeCNCo(CN)<inf>5</inf>]<sup>5-</sup> and [Fe(CN)<inf>6</inf>]<sup>3-</sup> Journal of the Chemical Society, Dalton Transactions. 1949-1953. DOI: 10.1039/DT9830001949  0.64
1983 Beoku-Betts D, Chapman SK, Knox CV, Sykes AG. Concerning the binding site on plastocyanin for its natural redox partner cytochrome f Journal of the Chemical Society, Chemical Communications. 1150-1152.  0.64
1983 Chapman SK, Davies DM, Vuik CPJ, Sykes AG. Electron-transfer reactions of cytochrome b5: Binding site for inorganic complexes and cytochrome c Journal of the Chemical Society, Chemical Communications. 868-869.  0.64
1983 Chapman SK, Sinclair-Day JD, Sykes AG, Tam SC, Williams RJP. The influence of charge on reactions of metalloproteins with small molecules Journal of the Chemical Society, Chemical Communications. 1152-1154.  0.64
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