Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Michael J. Lacasse"'
Autor:
Stephanie Sebastiampillai, Michael J Lacasse, Susan McCusker, Tracey Campbell, Mark Nitz, Deborah B Zamble
Publikováno v:
Metallomics. 14
[NiFe]-hydrogenases are used by several human pathogens to catalyze the reversible conversion between molecular hydrogen and protons and electrons. Hydrogenases provide an increased metabolic flexibility for pathogens, such as Escherichia coli and He
Autor:
Deborah B. Zamble, Michael J. Lacasse, Mozhgan Khorasani-Motlagh, Graham N. George, Kelly L. Summers
Publikováno v:
Inorganic Chemistry. 58:13604-13618
[NiFe]-hydrogenase enzymes catalyze the reversible oxidation of hydrogen at a bimetallic cluster and are used by bacteria and archaea for anaerobic growth and pathogenesis. Maturation of the [NiFe]-hydrogenase requires several accessory proteins to a
Autor:
Michael J, Lacasse, Kelly L, Summers, Mozhgan, Khorasani-Motlagh, Graham N, George, Deborah B, Zamble
Publikováno v:
Inorg Chem
[NiFe]-hydrogenase enzymes catalyze the reversible oxidation of hydrogen at a bimetallic active site and they are used by bacteria and archaea for anaerobic growth and pathogenesis. Maturation of the [NiFe]-hydrogenase requires several accessory prot
Autor:
Eric D. Brown, Michael J. Lacasse, Nicholas Hodkinson, Jean-Philippe Côté, Deborah B. Zamble, Stephanie Sebastiampillai
Publikováno v:
J Biol Chem
[NiFe]-hydrogenases have attracted attention as potential therapeutic targets or components of a hydrogen-based economy. [NiFe]-hydrogenase production is a complicated process that requires many associated accessory proteins that supply the requisite
Publikováno v:
Metallomics. 9:482-493
[NiFe]-hydrogenase, which catalyzes the reversible conversion between hydrogen gas and protons, is a vital component of the metabolism of many pathogens. Maturation of [NiFe]-hydrogenase requires selective nickel insertion that is completed, in part,
Publikováno v:
Biochemistry. 55(49)
[NiFe]-hydrogenase enzymes catalyze the reversible reduction of protons to molecular hydrogen and serve as a vital component of the metabolism of many pathogens. The synthesis of the bimetallic catalytic center requires a suite of accessory proteins,
Autor:
Deborah B. Zamble, Michael J. Lacasse
Publikováno v:
Biochemistry. 55(12)
[NiFe]-hydrogenases catalyze the reversible conversion of hydrogen gas into protons and electrons and are vital metabolic components of many species of bacteria and archaea. At the core of this enzyme is a sophisticated catalytic center comprising ni
Autor:
Steven K. Burger, Paul W. Ayers, Joel A. Drewry, Michael J. Lacasse, Toon Verstraelen, Patrick T. Gunning
Publikováno v:
Journal of Chemical Theory and Computation
A procedure for determining force constants that is independent of the internal redundant coordinate choice is presented. The procedure is based on solving each bond and angle term separately, using the Wilson B matrix. The method only requires a sin
Autor:
Michael J. Adam, Eszter Boros, Brian O. Patrick, Gwendolyn A. Bailey, Jason S. Lewis, Cara L. Ferreira, Brian M. Zeglis, Eric W. Price, Michael J. Lacasse, Chris Orvig
Publikováno v:
Inorganic chemistry. 51(22)
Preliminary experiments with the novel acyclic triazole-containing bifunctional chelator H2azapa and the radiometals (64)Cu, (67)Ga, (111)In, and (177)Lu have established its significant versatile potential as an alternative to 1,4,7,10-tetraazacyclo