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Your search keyword '"Mouesca, J.-M."' showing total 2 results
Start Over Author "Mouesca, J.-M." Topic escherichia coli
2 results on '"Mouesca, J.-M."'

1. X-ray structural, functional and computational studies of the O 2 -sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe-4S] cluster.

Author

Volbeda A, Mouesca JM, Darnault C, Roessler MM, Parkin A, Armstrong FA, and Fontecilla-Camps JC

Subjects
Crystallography, X-Ray, Escherichia coli Proteins chemistry, Hydrogenase chemistry, Iron-Sulfur Proteins chemistry, Models, Molecular, Oxygen chemistry, Escherichia coli enzymology, Escherichia coli Proteins metabolism, Hydrogenase metabolism, Iron-Sulfur Proteins metabolism, Oxygen metabolism
Abstract

The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni-Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.

Published
2018
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2. X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster.

Author

Volbeda, A., Mouesca, J. M., Darnault, C., Roessler, M. M., Parkin, A., Armstrong, F. A., and Fontecilla-Camps, J. C.

Subjects
ESCHERICHIA coli, HYDROGENASE, X-ray diffraction measurement, ELECTRON paramagnetic resonance spectroscopy, CRYSTAL structure, CHARGE exchange
Abstract

The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype. [ABSTRACT FROM AUTHOR]

Published
2018
Full Text
View/download PDF

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