The carbon monoxide inhibition of the proton-deuterium exchange activity of iron, nickel-iron and nickel-iron-selenium hydrogenases from Desulfovibrio vulgaris Hildenborough

1987 ◽  
Vol 15 (6) ◽  
pp. 1050-1051 ◽  
Author(s):  
GUY FAUQUE ◽  
YVES BERLIER ◽  
EUI S. CHOI ◽  
HARRY D. PECK ◽  
JEAN LE GALL ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Deuterium Exchange ◽  
Desulfovibrio Vulgaris ◽  
Nickel Iron ◽  
Iron Nickel ◽  
Desulfovibrio Vulgaris Hildenborough ◽  
Exchange Activity

Interaction of the active site of the Ni–Fe–Se hydrogenase from Desulfovibrio vulgaris Hildenborough with carbon monoxide and oxygen inhibitors

2010 ◽  
Vol 15 (8) ◽  
pp. 1285-1292 ◽  
Author(s):  
Cristina Gutiérrez-Sánchez ◽  
Olaf Rüdiger ◽  
Víctor M. Fernández ◽  
Antonio L. De Lacey ◽  
Marta Marques ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Active Site ◽  
Desulfovibrio Vulgaris ◽  
Desulfovibrio Vulgaris Hildenborough

Characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough

2018 ◽  
pp. 169-201 ◽  
Author(s):  
Sónia Zacarias ◽  
Marisela Vélez ◽  
Marcos Pita ◽  
Antonio L. De Lacey ◽  
Pedro M. Matias ◽  
...  
Keyword(s):  
Desulfovibrio Vulgaris ◽  
Desulfovibrio Vulgaris Hildenborough

scholarly journals Inhibition of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F by carbon monoxide: An FTIR and EPR spectroscopic study

2010 ◽  
Vol 1797 (2) ◽  
pp. 304-313 ◽  
Author(s):  
Maria-Eirini Pandelia ◽  
Hideaki Ogata ◽  
Leslie J. Currell ◽  
Marco Flores ◽  
Wolfgang Lubitz
Keyword(s):  
Carbon Monoxide ◽  
Spectroscopic Study ◽  
Desulfovibrio Vulgaris

scholarly journals Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Elizabeth C Wittenborn ◽  
Mériem Merrouch ◽  
Chie Ueda ◽  
Laura Fradale ◽  
Christophe Léger ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Carbon Fixation ◽  
Conformational Dynamics ◽  
Oxidative Degradation ◽  
Carbon Monoxide Dehydrogenase ◽  
Cysteine Residue ◽  
Desulfovibrio Vulgaris ◽  
Cluster Assembly ◽  
X Ray Crystallography ◽  
Reduction Of Co2

The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO2 to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have observed unprecedented conformational dynamics in the C-cluster of the CODH from Desulfovibrio vulgaris, providing the first view of an oxidized state of the cluster. Combined with supporting spectroscopic data, our structures reveal that this novel, oxidized cluster arrangement plays a role in avoiding irreversible oxidative degradation at the C-cluster. Furthermore, mutagenesis of a conserved cysteine residue that binds the C-cluster in the oxidized state but not in the reduced state suggests that the oxidized conformation could be important for proper cluster assembly, in particular Ni incorporation. Together, these results lay a foundation for future investigations of C-cluster activation and assembly, and contribute to an emerging paradigm of metallocluster plasticity.

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