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James Bryant Howard

Affiliations: 
University of Minnesota, Twin Cities, Minneapolis, MN 
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"James Howard"
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Parents

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Alexander N. Glazer grad student 1968 UCLA

Children

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Richard P. Swenson grad student 1979 UMN
Robert P. Hausinger grad student 1977-1982 University of Minnesota - Minneapolis (Cell Biology Tree)
Jon Karl Magnuson grad student 1986-1993
Douglas C. Rees post-doc 1981-1982 UMN

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Publications

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Warmack RA, Maggiolo AO, Orta A, et al. (2023) Structural consequences of turnover-induced homocitrate loss in nitrogenase. Nature Communications. 14: 1091
Spatzal T, Perez KA, Howard JB, et al. (2015) Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor. Elife. 4
Tezcan FA, Kaiser JT, Howard JB, et al. (2015) Structural evidence for asymmetrical nucleotide interactions in nitrogenase. Journal of the American Chemical Society. 137: 146-9
Spatzal T, Perez KA, Howard JB, et al. (2015) Author response: Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor Elife
Glazer AN, Kechris K, Howard JB. (2015) Distribution and Ecological Niches of Nitrogenases Biological Nitrogen Fixation. 87-98
Spatzal T, Perez KA, Einsle O, et al. (2014) Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase. Science (New York, N.Y.). 345: 1620-3
Yang KY, Haynes CA, Spatzal T, et al. (2014) Turnover-dependent inactivation of the nitrogenase MoFe-protein at high pH. Biochemistry. 53: 333-43
Howard JB, Kechris KJ, Rees DC, et al. (2013) Multiple amino acid sequence alignment nitrogenase component 1: insights into phylogenetics and structure-function relationships. Plos One. 8: e72751
Zhang L, Kaiser JT, Meloni G, et al. (2013) The sixteenth iron in the nitrogenase MoFe protein. Angewandte Chemie (International Ed. in English). 52: 10529-32
MAGNUSON JK, PAUSTIAN TD, SHAH VK, et al. (2010) ChemInform Abstract: Nitrogenase Iron-Molybdenum Cofactor Binding Site: Protein Conformational Changes Associated with Cofactor Binding. Cheminform. 28: no-no
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