A Volbeda
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Explore the profile of A Volbeda including associated specialties, affiliations and a list of published articles.
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20
Citations
611
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Recent Articles
1.
Volbeda A, Mouesca J, Darnault C, Roessler M, Parkin A, Armstrong F, et al.
Chem Commun (Camb)
. 2018 Jun;
54(52):7175-7178.
PMID: 29888350
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...
2.
Dupuy J, Darnault C, Brazzolotto X, Kuhn L, Moulis J, Volbeda A, et al.
Acta Crystallogr Sect F Struct Biol Cryst Commun
. 2006 Mar;
61(Pt 5):482-5.
PMID: 16511074
Iron-regulatory proteins (IRPs) 1 and 2 are closely related molecules involved in animal iron metabolism. Both proteins can bind to specific mRNA regions called iron-responsive elements and thereby control the...
3.
Charon M, Volbeda A, Chabriere E, Pieulle L, Fontecilla-Camps J
Curr Opin Struct Biol
. 1999 Dec;
9(6):663-9.
PMID: 10607667
The first crystal structure of pyruvate:ferredoxin oxidoreductase to be determined has provided significant new information on its structural organization and redox chemistry. Spectroscopic analyses of a radical reaction intermediate have...
4.
Chabriere E, Volbeda A, Fontecilla-Camps J, Roth M, Charon M
Acta Crystallogr D Biol Crystallogr
. 1999 Sep;
55(Pt 9):1546-54.
PMID: 10489442
The structure of the homodimeric 267 kDa pyruvate:ferredoxin oxidoreductase (PFOR) of Desulfovibrio africanus was solved with data from two crystals forms, both containing two monomers per asymmetric unit. Phases were...
5.
Garcin E, Vernede X, Hatchikian E, Volbeda A, Frey M, Fontecilla-Camps J
Structure
. 1999 Jun;
7(5):557-66.
PMID: 10378275
Background: [NiFeSe] hydrogenases are metalloenzymes that catalyze the reaction H2<-->2H+ + 2e-. They are generally heterodimeric, contain three iron-sulfur clusters in their small subunit and a nickel-iron-containing active site in...
6.
Chabriere E, Charon M, Volbeda A, Pieulle L, Hatchikian E, Fontecilla-Camps J
Nat Struct Biol
. 1999 Feb;
6(2):182-90.
PMID: 10048931
Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A, a crucial step in many metabolic pathways, is carried out in most aerobic organisms by the multienzyme complex pyruvate dehydrogenase. In most...
7.
Garcin E, MONTET Y, Volbeda A, Hatchikian C, Frey M, Fontecilla-Camps J
Biochem Soc Trans
. 1998 Oct;
26(3):396-401.
PMID: 9765886
No abstract available.
8.
Fontecilla-Camps J, Frey M, Garcin E, Hatchikian C, MONTET Y, Piras C, et al.
Biochimie
. 1998 Feb;
79(11):661-6.
PMID: 9479448
Hydrogenases are proteins which metabolize the most simple of chemical compounds, molecular hydrogen, according to the reaction H2<-->2H+ + 2e-. These enzymes are found in many microorganisms of great biotechnological...
9.
MONTET Y, Amara P, Volbeda A, Vernede X, Hatchikian E, Field M, et al.
Nat Struct Biol
. 1997 Jul;
4(7):523-6.
PMID: 9228943
The 2.54 A resolution structure of Ni-Fe hydrogenase has revealed the existence of hydrophobic channels connecting the molecular surface to the active site. A crystallographic analysis of xenon binding together...
10.
Volbeda A, Fontecilla-Camps J, Frey M
Curr Opin Struct Biol
. 1996 Dec;
6(6):804-12.
PMID: 8994881
Recently, the three-dimensional structures of several novel metalloenzymes have been solved. Of special interest are those containing uncommon and/or not well characterized metals such as molybdenum, tungsten, nickel, vanadium and...