| Year |
Citation |
Score |
| 2023 |
Shepherd RE, Kreinbrink AC, Njimoh CL, Vali SW, Lindahl PA. Yeast Mitochondria Import Aqueous Fe and, When Activated for Iron-Sulfur Cluster Assembly, Export or Release Low-Molecular-Mass Iron and Also Export Iron That Incorporates into Cytosolic Proteins. Journal of the American Chemical Society. 145: 13556-13569. PMID 37339084 DOI: 10.1021/jacs.2c13439 |
0.519 |
|
| 2023 |
Brawley HN, Kreinbrink AC, Hierholzer JD, Vali SW, Lindahl PA. Labile Iron Pool of Isolated Cytosol Likely Includes Fe-ATP and Fe-Citrate but not Fe-Glutathione or Aqueous Fe. Journal of the American Chemical Society. 145: 2104-2117. PMID 36661842 DOI: 10.1021/jacs.2c06625 |
0.523 |
|
| 2022 |
Vali SW, Lindahl PA. Low-temperature Mössbauer spectroscopy of organs from Fe-enriched HFE hemochromatosis mice: an iron-dependent threshold for generating hemosiderin. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 36512071 DOI: 10.1007/s00775-022-01975-y |
0.432 |
|
| 2022 |
Vali SW, Lindahl PA. Might non-transferrin-bound iron in blood plasma and sera be a non-proteinaceous high-molecular-mass Fe aggregate? The Journal of Biological Chemistry. 102667. PMID 36334631 DOI: 10.1016/j.jbc.2022.102667 |
0.449 |
|
| 2022 |
Lindahl PA, Vali SW. Mössbauer-based molecular-level decomposition of the Saccharomyces cerevisiae ironome, and preliminary characterization of isolated nuclei. Metallomics : Integrated Biometal Science. PMID 36214417 DOI: 10.1093/mtomcs/mfac080 |
0.396 |
|
| 2022 |
Fernandez S, Wofford JD, Shepherd RE, Vali SW, Dancis A, Lindahl PA. Yeast cells depleted of the frataxin homolog Yfh1 redistribute cellular iron: Studies using Mössbauer spectroscopy and mathematical modeling. The Journal of Biological Chemistry. 298: 101921. PMID 35413285 DOI: 10.1016/j.jbc.2022.101921 |
0.469 |
|
| 2021 |
Hyun SM, Reid KA, Vali SW, Lindahl PA, Powers DC. Cis-Divacant Octahedral Fe(II) in a Dimensionally Reduced Family of 2-(Pyridin-2-yl)pyrrolide Complexes. Inorganic Chemistry. PMID 34590844 DOI: 10.1021/acs.inorgchem.1c02240 |
0.333 |
|
| 2021 |
Drake HF, Xiao Z, Day GS, Vali SW, Chen W, Wang Q, Huang Y, Yan TH, Kuszynski JE, Lindahl PA, Ryder MR, Zhou HC. Thermal decarboxylation for the generation of hierarchical porosity in isostructural metal-organic frameworks containing open metal sites. Materials Advances. 2: 5487-5493. PMID 34458847 DOI: 10.1039/d1ma00163a |
0.429 |
|
| 2021 |
Vali SW, Haja DK, Brand RA, Adams MWW, Lindahl PA. The Pyrococcus furiosus ironome is dominated by [FeS] clusters or thioferrate-like iron depending on the availability of elemental sulfur. The Journal of Biological Chemistry. 100710. PMID 33930466 DOI: 10.1016/j.jbc.2021.100710 |
0.502 |
|
| 2020 |
Kim JE, Vali SW, Nguyen TQ, Dancis A, Lindahl PA. Mössbauer and LC-ICP-MS investigation of iron trafficking between vacuoles and mitochondria in Vma2Δ . The Journal of Biological Chemistry. PMID 33268384 DOI: 10.1074/jbc.RA120.015907 |
0.418 |
|
| 2020 |
Khan D, Lee D, Gulten G, Aggarwal A, Wofford J, Krieger I, Tripathi A, Patrick JW, Eckert DM, Laganowsky A, Sacchettini J, Lindahl P, Bankaitis VA. A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins. Elife. 9. PMID 32780017 DOI: 10.7554/Elife.57081 |
0.398 |
|
| 2020 |
Nguyen TQ, Kim JE, Brawley HN, Lindahl PA. Chromatographic detection of low-molecular-mass metal complexes in the cytosol of Saccharomyces cerevisiae. Metallomics : Integrated Biometal Science. PMID 32301942 DOI: 10.1039/C9Mt00312F |
0.302 |
|
| 2019 |
Soma S, Morgada MN, Naik MT, Boulet A, Roesler AA, Dziuba N, Ghosh A, Yu Q, Lindahl PA, Ames JB, Leary SC, Vila AJ, Gohil VM. COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase. Cell Reports. 29: 4114-4126.e5. PMID 31851937 DOI: 10.1016/J.Celrep.2019.11.054 |
0.304 |
|
| 2019 |
Dziuba N, Hardy J, Lindahl PA. Low-molecular-mass iron complexes in blood plasma of iron-deficient pigs do not originate directly from nutrient iron. Metallomics : Integrated Biometal Science. PMID 31603444 DOI: 10.1039/C9Mt00152B |
0.517 |
|
| 2019 |
Drake HF, Day GS, Vali SW, Xiao Z, Banerjee S, Li J, Joseph EA, Kuszynski JE, Perry ZT, Kirchon A, Ozdemir OK, Lindahl PA, Zhou HC. The thermally induced decarboxylation mechanism of a mixed-oxidation state carboxylate-based iron metal-organic framework. Chemical Communications (Cambridge, England). PMID 31565709 DOI: 10.1039/C9Cc04555D |
0.534 |
|
| 2019 |
Lindahl PA. A comprehensive mechanistic model of iron metabolism in Saccharomyces cerevisiae. Metallomics : Integrated Biometal Science. PMID 31531508 DOI: 10.1039/C9Mt00199A |
0.411 |
|
| 2019 |
Nguyen TQ, Dziuba N, Lindahl PA. Isolated Saccharomyces cerevisiae vacuoles contain low-molecular-mass transition-metal polyphosphate complexes. Metallomics : Integrated Biometal Science. PMID 31210222 DOI: 10.1039/C9Mt00104B |
0.322 |
|
| 2019 |
Wofford JD, Lindahl PA. A mathematical model of iron import and trafficking in wild-type and Mrs3/4ΔΔ yeast cells. Bmc Systems Biology. 13: 23. PMID 30791941 DOI: 10.1186/S12918-019-0702-2 |
0.475 |
|
| 2018 |
Wofford JD, Bolaji N, Dziuba N, Outten FW, Lindahl PA. Evidence that a respiratory shield in protects a low-molecular-mass Fe pool from O-dependent oxidation. The Journal of Biological Chemistry. PMID 30337367 DOI: 10.1074/Jbc.Ra118.005233 |
0.555 |
|
| 2018 |
Dziuba N, Hardy J, Lindahl PA. Low-molecular-mass iron in healthy blood plasma is not predominately ferric citrate. Metallomics : Integrated Biometal Science. PMID 29808889 DOI: 10.1039/C8Mt00055G |
0.438 |
|
| 2018 |
Pandey A, Pain J, Dziuba N, Pandey AK, Dancis A, Lindahl PA, Pain D. Mitochondria Export Sulfur Species Required for Cytosolic tRNA Thiolation. Cell Chemical Biology. PMID 29706592 DOI: 10.1016/J.Chembiol.2018.04.002 |
0.368 |
|
| 2018 |
Moore MJ, Wofford JD, Dancis A, Lindahl PA. Recovery of mrs3Δmrs4Δ Saccharomyces cerevisiae Cells under Iron-Sufficient Conditions and the Role of Fe580. Biochemistry. PMID 29228768 DOI: 10.1021/Acs.Biochem.7B01034 |
0.552 |
|
| 2017 |
Kuppuswamy S, Wofford JD, Joseph C, Xie ZL, Ali AK, Lynch VM, Lindahl PA, Rose MJ. Structures, Interconversions, and Spectroscopy of Iron Carbonyl Clusters with an Interstitial Carbide: Localized Metal Center Reduction by Overall Cluster Oxidation. Inorganic Chemistry. PMID 28605580 DOI: 10.1021/acs.inorgchem.7b01386 |
0.331 |
|
| 2017 |
Kuppuswamy S, Wofford JD, Joseph C, Xie ZL, Ali AK, Lynch VM, Lindahl PA, Rose MJ. Structures, Interconversions, and Spectroscopy of Iron Carbonyl Clusters with an Interstitial Carbide: Localized Metal Center Reduction by Overall Cluster Oxidation. Inorganic Chemistry. PMID 28441025 DOI: 10.1021/Acs.Inorgchem.7B00741 |
0.611 |
|
| 2017 |
Wofford JD, Chakrabarti M, Lindahl PA. Mössbauer Spectra of Mouse Hearts reveal age-dependent changes in mitochondrial and ferritin iron levels. The Journal of Biological Chemistry. PMID 28202542 DOI: 10.1074/Jbc.M117.777201 |
0.676 |
|
| 2016 |
Lindahl PA, Moore MJ. Labile Low-Molecular-Mass Metal Complexes in Mitochondria: Trials and Tribulations of a Burgeoning Field. Biochemistry. PMID 27433847 DOI: 10.1021/Acs.Biochem.6B00216 |
0.367 |
|
| 2016 |
Wofford JD, Park J, McCormick SP, Chakrabarti M, Lindahl PA. Ferric ions accumulate in the walls of metabolically inactivating Saccharomyces cerevisiae cells and are reductively mobilized during reactivation. Metallomics : Integrated Biometal Science. PMID 27188213 DOI: 10.1039/C6Mt00070C |
0.729 |
|
| 2015 |
Wofford JD, Lindahl PA. Mitochondrial Iron-Sulfur Cluster Activity and Cytosolic Iron Regulate Iron Traffic in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 290: 26968-77. PMID 26306041 DOI: 10.1074/Jbc.M115.676668 |
0.558 |
|
| 2015 |
McCormick SP, Moore MJ, Lindahl PA. Detection of Labile Low-Molecular-Mass Transition Metal Complexes in Mitochondria. Biochemistry. 54: 3442-53. PMID 26018429 DOI: 10.1021/Bi5015437 |
0.472 |
|
| 2015 |
Fox NG, Das D, Chakrabarti M, Lindahl PA, Barondeau DP. Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex. Biochemistry. PMID 26016518 DOI: 10.1021/Bi5014497 |
0.842 |
|
| 2015 |
Fox NG, Chakrabarti M, McCormick SP, Lindahl PA, Barondeau DP. The Human Iron-Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor Molecules. Biochemistry. 54: 3871-9. PMID 26016389 DOI: 10.1021/Bi5014485 |
0.84 |
|
| 2015 |
Chakrabarti M, Barlas MN, McCormick SP, Lindahl LS, Lindahl PA. Kinetics of iron import into developing mouse organs determined by a pup-swapping method. The Journal of Biological Chemistry. 290: 520-8. PMID 25371212 DOI: 10.1074/Jbc.M114.606731 |
0.687 |
|
| 2015 |
Chakrabarti M, Cockrell AL, Park J, McCormick SP, Lindahl LS, Lindahl PA. Speciation of iron in mouse liver during development, iron deficiency, IRP2 deletion and inflammatory hepatitis. Metallomics : Integrated Biometal Science. 7: 93-101. PMID 25325718 DOI: 10.1039/C4Mt00215F |
0.717 |
|
| 2015 |
Fox NG, Chakrabarti M, McCormick SP, Lindahl PA, Barondeau DP. The Human Iron-Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor Molecules Biochemistry. 54: 3871-3879. DOI: 10.1021/bi5014485 |
0.819 |
|
| 2014 |
Park J, McCormick SP, Cockrell AL, Chakrabarti M, Lindahl PA. High-spin ferric ions in Saccharomyces cerevisiae vacuoles are reduced to the ferrous state during adenine-precursor detoxification. Biochemistry. 53: 3940-51. PMID 24919141 DOI: 10.1021/Bi500148Y |
0.734 |
|
| 2014 |
Cockrell A, McCormick SP, Moore MJ, Chakrabarti M, Lindahl PA. Mössbauer, EPR, and modeling study of iron trafficking and regulation in Δccc1 and CCC1-up Saccharomyces cerevisiae. Biochemistry. 53: 2926-40. PMID 24785783 DOI: 10.1021/Bi500002N |
0.725 |
|
| 2013 |
Park J, McCormick SP, Chakrabarti M, Lindahl PA. The lack of synchronization between iron uptake and cell growth leads to iron overload in Saccharomyces cerevisiae during post-exponential growth modes. Biochemistry. 52: 9413-25. PMID 24344915 DOI: 10.1021/Bi4010304 |
0.718 |
|
| 2013 |
Jhurry ND, Chakrabarti M, McCormick SP, Gohil VM, Lindahl PA. Mössbauer study and modeling of iron import and trafficking in human jurkat cells. Biochemistry. 52: 7926-42. PMID 24180611 DOI: 10.1021/Bi401015T |
0.722 |
|
| 2013 |
Park J, McCormick SP, Chakrabarti M, Lindahl PA. Insights into the iron-ome and manganese-ome of Δmtm1 Saccharomyces cerevisiae mitochondria. Metallomics : Integrated Biometal Science. 5: 656-72. PMID 23598994 DOI: 10.1039/C3Mt00041A |
0.726 |
|
| 2013 |
McCormick SP, Chakrabarti M, Cockrell AL, Park J, Lindahl LS, Lindahl PA. Low-molecular-mass metal complexes in the mouse brain. Metallomics : Integrated Biometal Science. 5: 232-41. PMID 23443205 DOI: 10.1039/C3Mt00009E |
0.578 |
|
| 2013 |
Holmes-Hampton GP, Jhurry ND, McCormick SP, Lindahl PA. Iron content of Saccharomyces cerevisiae cells grown under iron-deficient and iron-overload conditions. Biochemistry. 52: 105-14. PMID 23253189 DOI: 10.1021/Bi3015339 |
0.818 |
|
| 2012 |
Holmes-Hampton GP, Chakrabarti M, Cockrell AL, McCormick SP, Abbott LC, Lindahl LS, Lindahl PA. Changing iron content of the mouse brain during development. Metallomics : Integrated Biometal Science. 4: 761-70. PMID 22810488 DOI: 10.1039/C2Mt20086D |
0.835 |
|
| 2012 |
Jhurry ND, Chakrabarti M, McCormick SP, Holmes-Hampton GP, Lindahl PA. Biophysical investigation of the ironome of human jurkat cells and mitochondria. Biochemistry. 51: 5276-84. PMID 22726227 DOI: 10.1021/Bi300382D |
0.848 |
|
| 2012 |
Schilter D, Nilges MJ, Chakrabarti M, Lindahl PA, Rauchfuss TB, Stein M. Mixed-valence nickel-iron dithiolate models of the [NiFe]-hydrogenase active site. Inorganic Chemistry. 51: 2338-48. PMID 22304696 DOI: 10.1021/Ic202329Y |
0.69 |
|
| 2012 |
Lindahl PA. Metal-metal bonds in biology. Journal of Inorganic Biochemistry. 106: 172-8. PMID 22119810 DOI: 10.1016/J.Jinorgbio.2011.08.012 |
0.447 |
|
| 2011 |
Cockrell AL, Holmes-Hampton GP, McCormick SP, Chakrabarti M, Lindahl PA. Mössbauer and EPR study of iron in vacuoles from fermenting Saccharomyces cerevisiae. Biochemistry. 50: 10275-83. PMID 22047049 DOI: 10.1021/Bi2014954 |
0.838 |
|
| 2011 |
Kamat SS, Holmes-Hampton GP, Bagaria A, Kumaran D, Tichy SE, Gheyi T, Zheng X, Bain K, Groshong C, Emtage S, Sauder JM, Burley SK, Swaminathan S, Lindahl PA, Raushel FM. The catalase activity of diiron adenine deaminase. Protein Science : a Publication of the Protein Society. 20: 2080-94. PMID 21998098 DOI: 10.1002/Pro.748 |
0.776 |
|
| 2011 |
Miao R, Holmes-Hampton GP, Lindahl PA. Biophysical investigation of the iron in Aft1-1(up) and Gal-YAH1 Saccharomyces cerevisiae. Biochemistry. 50: 2660-71. PMID 21361388 DOI: 10.1021/Bi102015S |
0.846 |
|
| 2011 |
Lindahl PA, Holmes-Hampton GP. Biophysical probes of iron metabolism in cells and organelles. Current Opinion in Chemical Biology. 15: 342-6. PMID 21282072 DOI: 10.1016/J.Cbpa.2011.01.007 |
0.808 |
|
| 2011 |
Kamat SS, Bagaria A, Kumaran D, Holmes-Hampton GP, Fan H, Sali A, Sauder JM, Burley SK, Lindahl PA, Swaminathan S, Raushel FM. Catalytic mechanism and three-dimensional structure of adenine deaminase. Biochemistry. 50: 1917-27. PMID 21247091 DOI: 10.1021/Bi101788N |
0.777 |
|
| 2010 |
Garber Morales J, Holmes-Hampton GP, Miao R, Guo Y, Münck E, Lindahl PA. Biophysical characterization of iron in mitochondria isolated from respiring and fermenting yeast. Biochemistry. 49: 5436-44. PMID 20536189 DOI: 10.1021/Bi100558Z |
0.851 |
|
| 2010 |
Holmes-Hampton GP, Miao R, Garber Morales J, Guo Y, Münck E, Lindahl PA. A nonheme high-spin ferrous pool in mitochondria isolated from fermenting Saccharomyces cerevisiae. Biochemistry. 49: 4227-34. PMID 20408527 DOI: 10.1021/Bi1001823 |
0.836 |
|
| 2009 |
Lindahl PA. Nickel-carbon bonds in acetyl-coenzyme a synthases/carbon monoxide dehydrogenases. Metal Ions in Life Sciences. 6: 133-50. PMID 20877794 DOI: 10.1039/9781847559333-00133 |
0.403 |
|
| 2009 |
Miao R, Kim H, Koppolu UM, Ellis EA, Scott RA, Lindahl PA. Biophysical characterization of the iron in mitochondria from Atm1p-depleted Saccharomyces cerevisiae. Biochemistry. 48: 9556-68. PMID 19761223 DOI: 10.1021/Bi901110N |
0.749 |
|
| 2009 |
Volbeda A, Darnault C, Tan X, Lindahl PA, Fontecilla-Camps JC. Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica. Biochemistry. 48: 7916-26. PMID 19650626 DOI: 10.1021/Bi9003952 |
0.402 |
|
| 2009 |
Lindahl PA, Morales JG, Miao R, Holmes-Hampton G. Chapter 15 Isolation of Saccharomyces cerevisiae mitochondria for Mössbauer, EPR, and electronic absorption spectroscopic analyses. Methods in Enzymology. 456: 267-85. PMID 19348894 DOI: 10.1016/S0076-6879(08)04415-7 |
0.817 |
|
| 2008 |
Miao R, Martinho M, Morales JG, Kim H, Ellis EA, Lill R, Hendrich MP, Münck E, Lindahl PA. EPR and Mössbauer spectroscopy of intact mitochondria isolated from Yah1p-depleted Saccharomyces cerevisiae. Biochemistry. 47: 9888-99. PMID 18717590 DOI: 10.1021/Bi801047Q |
0.793 |
|
| 2008 |
Tan X, Martinho M, Stubna A, Lindahl PA, Münck E. Mossbauer evidence for an exchange-coupled {[Fe4S4]1+ Nip1+} A-cluster in isolated alpha subunits of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase. Journal of the American Chemical Society. 130: 6712-3. PMID 18459773 DOI: 10.1021/Ja801981H |
0.802 |
|
| 2008 |
Lindahl PA. Implications of a carboxylate-bound C-cluster structure of carbon monoxide dehydrogenase. Angewandte Chemie (International Ed. in English). 47: 4054-6. PMID 18404747 DOI: 10.1002/Anie.200800223 |
0.322 |
|
| 2008 |
Tan X, Lindahl PA. Tunnel mutagenesis and Ni-dependent reduction and methylation of the alpha subunit of acetyl coenzyme A synthase/carbon monoxide dehydrogenase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 771-8. PMID 18365259 DOI: 10.1007/S00775-008-0363-X |
0.423 |
|
| 2007 |
Tan X, Kagiampakis I, Surovtsev IV, Demeler B, Lindahl PA. Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Biochemistry. 46: 11606-13. PMID 17887777 DOI: 10.1021/Bi7014663 |
0.331 |
|
| 2007 |
Hudder BN, Morales JG, Stubna A, Münck E, Hendrich MP, Lindahl PA. Electron paramagnetic resonance and Mössbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 1029-53. PMID 17665226 DOI: 10.1007/S00775-007-0275-1 |
0.805 |
|
| 2007 |
Garber-Morales J, Miao R, Hudder BN, Stubna A, Münck E, Hendrich MP, Lindahl PA. 90 Biophysical probes of iron metabolism in mitochondria Mitochondrion. 7: 430. DOI: 10.1016/J.Mito.2007.08.094 |
0.752 |
|
| 2007 |
Lindahl PA, Graham DE. Acetyl-coenzyme A Synthases and Nickel-Containing Carbon Monoxide Dehydrogenases Nickel and Its Surprising Impact in Nature. 2: 357-415. DOI: 10.1002/9780470028131.ch9 |
0.309 |
|
| 2006 |
Tan X, Surovtsev IV, Lindahl PA. Kinetics of CO insertion and acetyl group transfer steps, and a model of the acetyl-CoA synthase catalytic mechanism. Journal of the American Chemical Society. 128: 12331-8. PMID 16967985 DOI: 10.1021/Ja0627702 |
0.356 |
|
| 2006 |
Bramlett MR, Stubna A, Tan X, Surovtsev IV, Münck E, Lindahl PA. Mössbauer and EPR study of recombinant acetyl-CoA synthase from Moorella thermoacetica. Biochemistry. 45: 8674-85. PMID 16834342 DOI: 10.1021/Bi060003+ |
0.79 |
|
| 2006 |
Tan X, Volbeda A, Fontecilla-Camps JC, Lindahl PA. Function of the tunnel in acetylcoenzyme A synthase/carbon monoxide dehydrogenase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 371-8. PMID 16502006 DOI: 10.1007/S00775-006-0086-9 |
0.429 |
|
| 2005 |
Tan X, Loke HK, Fitch S, Lindahl PA. The tunnel of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase regulates delivery of CO to the active site. Journal of the American Chemical Society. 127: 5833-9. PMID 15839681 DOI: 10.1021/Ja043701V |
0.675 |
|
| 2004 |
Feng J, Lindahl PA. Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases. Journal of the American Chemical Society. 126: 9094-100. PMID 15264843 DOI: 10.1021/Ja048811G |
0.458 |
|
| 2004 |
Lindahl PA. Acetyl-coenzyme A synthase: the case for a Ni(p)(0)-based mechanism of catalysis. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 516-24. PMID 15221478 DOI: 10.1007/S00775-004-0564-X |
0.49 |
|
| 2004 |
Tan X, Bramlett MR, Lindahl PA. Effect of Zn on acetyl coenzyme a synthase: evidence for a conformational change in the alpha subunit during catalysis. Journal of the American Chemical Society. 126: 5954-5. PMID 15137746 DOI: 10.1021/Ja039600Z |
0.352 |
|
| 2004 |
Kim EJ, Feng J, Bramlett MR, Lindahl PA. Evidence for a proton transfer network and a required persulfide-bond-forming cysteine residue in Ni-containing carbon monoxide dehydrogenases. Biochemistry. 43: 5728-34. PMID 15134447 DOI: 10.1021/Bi036062U |
0.378 |
|
| 2004 |
Webster CE, Darensbourg MY, Lindahl PA, Hall MB. Structures and Energetics of Models for the Active Site of Acetyl-Coenzyme A Synthase: Role of Distal and Proximal Metals in Catalysis Journal of the American Chemical Society. 126: 3410-3411. PMID 15025453 DOI: 10.1021/Ja038083H |
0.32 |
|
| 2004 |
Maynard EL, Tan X, Lindahl PA. Autocatalytic activation of acetyl-CoA synthase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 316-22. PMID 15015040 DOI: 10.1007/S00775-004-0528-1 |
0.759 |
|
| 2004 |
Feng J, Lindahl PA. Carbon monoxide dehydrogenase from Rhodospirillum rubrum: effect of redox potential on catalysis. Biochemistry. 43: 1552-9. PMID 14769031 DOI: 10.1021/Bi0357199 |
0.408 |
|
| 2003 |
Bramlett MR, Tan X, Lindahl PA. Inactivation of acetyl-CoA synthase/carbon monoxide dehydrogenase by copper. Journal of the American Chemical Society. 125: 9316-7. PMID 12889960 DOI: 10.1021/Ja0352855 |
0.382 |
|
| 2003 |
Darnault C, Volbeda A, Kim EJ, Legrand P, Vernède X, Lindahl PA, Fontecilla-Camps JC. Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nature Structural Biology. 10: 271-9. PMID 12627225 DOI: 10.1038/Nsb912 |
0.454 |
|
| 2003 |
Loke HK, Lindahl PA. Identification and preliminary characterization of AcsF, a putative Ni-insertase used in the biosynthesis of acetyl-CoA synthase from Clostridium thermoaceticum. Journal of Inorganic Biochemistry. 93: 33-40. PMID 12538050 DOI: 10.1016/S0162-0134(02)00457-9 |
0.751 |
|
| 2003 |
Tan X, Sewell C, Yang Q, Lindahl PA. Reduction and methyl transfer kinetics of the alpha subunit from acetyl coenzyme a synthase. Journal of the American Chemical Society. 125: 318-9. PMID 12517128 DOI: 10.1021/Ja028442T |
0.387 |
|
| 2002 |
Lindahl PA. Stoichiometric redox titrations of complex metalloenzymes. Methods in Enzymology. 354: 296-309. PMID 12418235 DOI: 10.1016/S0076-6879(02)54024-6 |
0.34 |
|
| 2002 |
Loke HK, Tan X, Lindahl PA. Genetic construction of truncated and chimeric metalloproteins derived from the alpha subunit of acetyl-CoA synthase from Clostridium thermoaceticum. Journal of the American Chemical Society. 124: 8667-72. PMID 12121109 DOI: 10.1021/Ja025924W |
0.736 |
|
| 2002 |
Tan XS, Sewell C, Lindahl PA. Stopped-Flow Kinetics of Methyl Group Transfer between the Corrinoid-Iron-Sulfur Protein and Acetyl-Coenzyme A Synthase from Clostridium thermoaceticum. Journal of the American Chemical Society. 124: 6277-84. PMID 12033855 DOI: 10.1021/Ja016676R |
0.333 |
|
| 2001 |
Maynard EL, Lindahl PA. Catalytic coupling of the active sites in acetyl-CoA synthase, a bifunctional CO-channeling enzyme. Biochemistry. 40: 13262-7. PMID 11683635 DOI: 10.1021/Bi015604+ |
0.74 |
|
| 2001 |
Lindahl PA, Chang B. The evolution of acetyl-CoA synthase Origins of Life and Evolution of the Biosphere. 31: 403-434. PMID 11599178 DOI: 10.1023/A:1011809430237 |
0.31 |
|
| 2001 |
Maynard EL, Sewell C, Lindahl PA. Kinetic mechanism of acetyl-CoA synthase: steady-state synthesis at variable Co/Co2 pressures. Journal of the American Chemical Society. 123: 4697-703. PMID 11457278 DOI: 10.1021/Ja004017T |
0.71 |
|
| 2000 |
Loke HK, Bennett GN, Lindahl PA. Active acetyl-CoA synthase from Clostridium thermoaceticum obtained by cloning and heterologous expression of acsAB in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 97: 12530-5. PMID 11050160 DOI: 10.1073/Pnas.220404397 |
0.752 |
|
| 1999 |
Wilson BE, Lindahl PA. Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 4: 742-8. PMID 10631605 DOI: 10.1007/S007750050346 |
0.357 |
|
| 1999 |
Fraser DM, Lindahl PA. Evidence for a proposed intermediate redox state in the CO/CO(2) active site of acetyl-CoA synthase (Carbon monoxide dehydrogenase) from Clostridium thermoaceticum. Biochemistry. 38: 15706-11. PMID 10625436 DOI: 10.1021/Bi990398F |
0.342 |
|
| 1999 |
Fraser DM, Lindahl PA. Stoichiometric CO reductive titrations of acetyl-CoA synthase (Carbon monoxide dehydrogenase) from Clostridium thermoaceticum. Biochemistry. 38: 15697-705. PMID 10625435 DOI: 10.1021/Bi990397N |
0.345 |
|
| 1999 |
Maynard EL, Lindahl PA. Evidence of a molecular tunnel connecting the active sites for Co2 reduction and acetyl-CoA synthesis in acetyl-CoA synthase from Clostridium thermoaceticum [2] Journal of the American Chemical Society. 121: 9221-9222. DOI: 10.1021/Ja992120G |
0.754 |
|
| 1998 |
Russell WK, Lindahl PA. CO/CO2 potentiometric titrations of carbon monoxide dehydrogenase from Clostridium thermoaceticum and the effect of CO2 Biochemistry. 37: 10016-10026. PMID 9665707 DOI: 10.1021/Bi980149B |
0.407 |
|
| 1998 |
Russell WK, Stålhandske CMV, Xia J, Scott RA, Lindahl PA. Spectroscopic, redox, and structural characterization of the Ni-labile and nonlabile forms of the acetyl-CoA synthase active site of carbon monoxide dehydrogenase Journal of the American Chemical Society. 120: 7502-7510. DOI: 10.1021/Ja981165Z |
0.436 |
|
| 1998 |
DeRose VJ, Telser J, Anderson ME, Lindahl PA, Hoffman BM. A multinuclear ENDOR study of the C-cluster in CO dehydrogenase from Clostridium thermoaceticum: Evidence for H(x)O and histidine coordination to the [Fe4S4] center Journal of the American Chemical Society. 120: 8767-8776. DOI: 10.1021/Ja9731480 |
0.451 |
|
| 1997 |
Xia J, Hu Z, Popescu CV, Lindahl PA, Münck E. Mossbauer and EPR study of the Ni-activated α-subunit of carbon monoxide dehydrogenase from Clostridium thermoaceticum Journal of the American Chemical Society. 119: 8301-8312. DOI: 10.1021/Ja971025+ |
0.818 |
|
| 1997 |
Barondeau DP, Lindahl PA. Methylation of carbon monoxide dehydrogenase from Clostridium thermoaceticum and mechanism of acetyl coenzyme A synthesis Journal of the American Chemical Society. 119: 3959-3970. DOI: 10.1021/Ja963597K |
0.724 |
|
| 1996 |
Anderson ME, Lindahl PA. Spectroscopic states of the CO oxidation/CO2 reduction active site of carbon monoxide dehydrogenase and mechanistic implications Biochemistry. 35: 8371-8380. PMID 8679595 DOI: 10.1021/Bi952902W |
0.402 |
|
| 1996 |
Xia J, Sinclair JF, Baldwin TO, Lindahl PA. Carbon monoxide dehydrogenase from Clostridium thermoaceticum: Quaternary structure, stoichiometry of its SDS-induced dissociation, and characterization of the faster-migrating form Biochemistry. 35: 1965-1971. PMID 8639680 DOI: 10.1021/Bi9511853 |
0.454 |
|
| 1996 |
Spangler NJ, Lindahl PA, Bandarian V, Ludden PW. Spectroelectrochemical characterization of the metal centers in carbon monoxide dehydrogenase (CODH) and nickel-deficient CODH from Rhodospirillum rubrum Journal of Biological Chemistry. 271: 7973-7977. PMID 8626477 DOI: 10.1074/Jbc.271.14.7973 |
0.406 |
|
| 1996 |
Xia J, Lindahl PA. Assembly of an exchange-coupled [Ni:Fe4S4] cluster in the α metallosubunit of carbon monoxide dehydrogenase from Clostridium thermoaceticum with spectroscopic properties and CO-binding ability mimicking those of the acetyl-CoA synthase active site Journal of the American Chemical Society. 118: 483-484. DOI: 10.1021/Ja952845U |
0.36 |
|
| 1996 |
Hu Z, Spangler NJ, Anderson ME, Xia J, Ludden PW, Lindahl PA, Münck E. Nature of the C-cluster in Ni-containing carbon monoxide dehydrogenases Journal of the American Chemical Society. 118: 830-844. DOI: 10.1021/Ja9528386 |
0.635 |
|
| 1995 |
Roberts LM, Lindahl PA. Stoichiometric reductive titrations of Desulfovibrio gigas hydrogenase Journal of the American Chemical Society. 117: 2565-2572. DOI: 10.1021/Ja00114A020 |
0.396 |
|
| 1995 |
Xia J, Hu E, Anderson ME, Barondeau DP, Russell WK, Sinclair J, Dong J, Wang S, Scott RA, Baldwin TO, Münck E, Lindahl PA. The nickel and iron-sulfur centers in carbon monoxide dehydrogenase Journal of Inorganic Biochemistry. 59: 634. DOI: 10.1016/0162-0134(95)97723-4 |
0.778 |
|
| 1995 |
Xia J, Dong J, Wang S, Scott RA, Lindahl PA. EXAFS, EPR, and electronic absorption spectroscopic study of the α metallosubunit of CO dehydrogenase from Clostridium thermoaceticum Journal of the American Chemical Society. 117: 7065-7070. |
0.41 |
|
| 1994 |
Anderson ME, Lindahl PA. Organization of clusters and internal electron pathways in CO dehydrogenase from Clostridium thermoaceticum: Relevance to the mechanism of catalysis and cyanide inhibition Biochemistry. 33: 8702-8711. PMID 8038160 DOI: 10.1021/Bi00195A011 |
0.43 |
|
| 1994 |
Roberts LM, Lindahl PA. Analysis of oxidative titrations of Desulfovibrio gigas hydrogenase; implications for the catalytic mechanism Biochemistry. 33: 14339-14350. PMID 7947844 DOI: 10.1021/Bi00251A048 |
0.408 |
|
| 1994 |
Barondeau DP, Roberts LM, Lindahl PA. Stability of the Ni-C state and oxidative titrations of Desulfovibrio gigas hydrogenase monitored by EPR and electronic absorption spectroscopies Journal of the American Chemical Society. 116: 3442-3448. DOI: 10.1021/Ja00087A033 |
0.762 |
|
| 1993 |
Shin W, Lindahl PA. Low spin quantitation of NiFeC EPR signal from carbon monoxide dehydrogenase is not due to damage incurred during protein purification Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1161: 317-322. PMID 8381672 DOI: 10.1016/0167-4838(93)90231-F |
0.379 |
|
| 1993 |
Chae MY, Omburo GA, Lindahl PA, Raushel FM. Antiferromagnetic coupling in the binuclear metal cluster of manganese-substituted phosphotriesterase Journal of the American Chemical Society. 115: 12173-12174. DOI: 10.1021/Ja00078A069 |
0.336 |
|
| 1993 |
Shin W, Anderson ME, Lindahl PA. Heterogeneous nickel environments in carbon monoxide dehydrogenase from Clostridium thermoaceticum Journal of the American Chemical Society. 115: 5522-5526. DOI: 10.1021/Ja00066A021 |
0.399 |
|
| 1993 |
Farmer PJ, Reibenspies JH, Lindahl PA, Darensbourg MY. Effects of sulfur site modification on the redox potentials of derivatives of [N,N′- Bis(2-mercaptoethyl)-1,5 -diazacyclooctanato] nickel(II) Journal of the American Chemical Society. 115: 4665-4674. DOI: 10.1021/Ja00064A030 |
0.333 |
|
| 1993 |
Barondeau DP, Roberts L, Lindahl PA. Oxidative titrations of Desulfovibrio gigas hydrogen monitored by EPR and electronic absorption spectroscopies Journal of Inorganic Biochemistry. 51: 53. DOI: 10.1016/0162-0134(93)85091-L |
0.665 |
|
| 1993 |
Roberts L, Barondeau D, Lindahl P. Stability and redox potential of NiC from nickel—iron hydrogenase Journal of Inorganic Biochemistry. 51: 52. DOI: 10.1016/0162-0134(93)85090-U |
0.666 |
|
| 1992 |
Shin W, Lindahl PA. Function and CO binding properties of the NiFe complex in carbon monoxide dehydrogenase from Clostridium thermoaceticum Biochemistry®. 31: 12870-12875. PMID 1334436 DOI: 10.1021/Bi00166A023 |
0.329 |
|
| 1992 |
Shin W, Stafford PR, Lindahl PA. Redox titrations of carbon monoxide dehydrogenase from Clostridium thermoaceticum Biochemistry. 31: 6003-6011. PMID 1320927 DOI: 10.1021/Bi00141A007 |
0.516 |
|
| 1990 |
Lindahl PA, Ragsdale SW, Münck E. Mössbauer study of CO dehydrogenase from Clostridium thermoaceticum. The Journal of Biological Chemistry. 265: 3880-8. PMID 2303484 |
0.676 |
|
| 1990 |
Lindahl PA, Münck E, Ragsdale SW. CO dehydrogenase from Clostridium thermoaceticum. EPR and electrochemical studies in CO2 and argon atmospheres. The Journal of Biological Chemistry. 265: 3873-9. PMID 2154491 |
0.525 |
|
| 1990 |
Lindahl PA, Kovacs JA. Reactivities and biological functions of iron-sulfur clusters Journal of Cluster Science. 1: 29-73. DOI: 10.1007/Bf00703585 |
0.462 |
|
| 1988 |
Lindahl PA, Papaefthymiou V, Orme-Johnson WH, Münck E. Mössbauer studies of solid thionin-oxidized MoFe protein of nitrogenase. The Journal of Biological Chemistry. 263: 19412-8. PMID 2848826 |
0.672 |
|
| 1987 |
Day EP, Kent TA, Lindahl PA, Münck E, Orme-Johnson WH, Roder H, Roy A. SQUID measurement of metalloprotein magnetization. New methods applied to the nitrogenase proteins. Biophysical Journal. 52: 837-53. PMID 3480761 DOI: 10.1016/S0006-3495(87)83277-0 |
0.642 |
|
| 1987 |
Lindahl PA, Gorelick NJ, Münck E, Orme-Johnson WH. EPR and Mössbauer studies of nucleotide-bound nitrogenase iron protein from Azotobacter vinelandii. The Journal of Biological Chemistry. 262: 14945-53. PMID 2822707 |
0.685 |
|
| 1987 |
Ragsdale SW, Lindahl PA, Münck E. Mössbauer, EPR, and optical studies of the corrinoid/iron-sulfur protein involved in the synthesis of acetyl coenzyme A by Clostridium thermoaceticum Journal of Biological Chemistry. 262: 14289-14297. PMID 2821001 |
0.479 |
|
| 1987 |
Lindahl PA, Teo BK, Orme-Johnson WH. EXAFS studies of the nitrogenase iron protein from Azotobacter vinelandii Inorganic Chemistry. 26: 3912-3916. DOI: 10.1021/Ic00270A018 |
0.645 |
|
| 1985 |
Lindahl PA, Day EP, Kent TA, Orme-Johnson WH, Münck E. Mössbauer, EPR, and magnetization studies of the Azotobacter vinelandii Fe protein. Evidence for a [4Fe-4S]1+ cluster with spin S = 3/2. The Journal of Biological Chemistry. 260: 11160-73. PMID 2993304 |
0.667 |
|
| 1984 |
Lindahl PA, Kojima N, Hausinger RP, Fox JA, Teo BK, Walsh CT, Orme-Johnson WH. Nickel and iron EXAFS of F420-reducing hydrogenase from Methanobacterium thermoautotrophicum Journal of the American Chemical Society. 106: 3062-3064. DOI: 10.1021/Ja00322A068 |
0.621 |
|
| 1983 |
Antonio M, Teo B, Orme-Johnson W, Lindahl P, Averill B. Iron EXAFS studies of the ironmolybdenum cofactor of nitrogenase and the 3Fe ferredoxin II of desulfovibrio gigas Inorganica Chimica Acta. 79: 88-89. DOI: 10.1016/S0020-1693(00)95121-1 |
0.8 |
|
| 1982 |
Antonio MR, Teo BK, Orme-Johnson WH, Nelson MJ, Groh SE, Lindahl PA, Kauzlarich SM, Averill BA. Iron EXAFS of the iron-molybdenum cofactor of nitrogenase Journal of the American Chemical Society. 104: 4703-4705. DOI: 10.1021/Ja00381A045 |
0.743 |
|
| 1982 |
Antonio MR, Teo BK, Orme-Johnson WH, Nelson MJ, Groh SE, Lindahl PA, Kauzlarich SM, Averill BA. Iron EXAFS of the iron-molybdenum cofactor of nitrogenase Journal of the American Chemical Society. 104: 4703-4705. DOI: 10.1021/ja00381a045 |
0.725 |
|
| Show low-probability matches. |