scholarly journals Protonation of Nickel–Iron Hydrogenase Models Proceeds after Isomerization at Nickel

2014 ◽  
Vol 136 (35) ◽  
pp. 12385-12395 ◽  
Author(s):  
Mioy T. Huynh ◽  
David Schilter ◽  
Sharon Hammes-Schiffer ◽  
Thomas B. Rauchfuss
Keyword(s):  
Nickel Iron Hydrogenase ◽  
Nickel Iron ◽  
Iron Hydrogenase

scholarly journals Reduction of Technetium(VII) byDesulfovibrio fructosovorans Is Mediated by the Nickel-Iron Hydrogenase

2001 ◽  
Vol 67 (10) ◽  
pp. 4583-4587 ◽  
Author(s):  
Gilles De Luca ◽  
Pascale de Philip ◽  
Zorah Dermoun ◽  
Marc Rousset ◽  
André Verméglio
Keyword(s):  
Resting Cells ◽  
Nickel Iron Hydrogenase ◽  
Nickel Iron ◽  
Sulfate Reducing ◽  
Cell Extracts ◽  
Black Precipitate ◽  
Iron Hydrogenase ◽  
Reducing Activity ◽  
Reducing Bacteria

ABSTRACT Resting cells of the sulfate-reducing bacteriumDesulfovibrio fructosovorans grown in the absence of sulfate had a very high Tc(VII)-reducing activity, which led to the formation of an insoluble black precipitate. The involvement of a periplasmic hydrogenase in Tc(VII) reduction was indicated (i) by the requirement for hydrogen as an electron donor, (ii) by the tolerance of this activity to oxygen, and (iii) by the inhibition of this activity by Cu(II). Moreover, a mutant carrying a deletion in the nickel-iron hydrogenase operon showed a dramatic decrease in the rate of Tc(VII) reduction. The restoration of Tc(VII) reduction by complementation of this mutation with nickel-iron hydrogenase genes demonstrated the specific involvement of the periplasmic nickel-iron hydrogenase in the mechanism in vivo. The Tc(VII)-reducing activity was also observed with cell extracts in the presence of hydrogen. Under these conditions, Tc(VII) was reduced enzymatically to soluble Tc(V) or precipitated to an insoluble black precipitate, depending on the chemical nature of the buffer used. The purified nickel-iron hydrogenase performed Tc(VII) reduction and precipitation at high rates. These series of genetic and biochemical approaches demonstrated that the periplasmic nickel-iron hydrogenase of sulfate-reducing bacteria functions as a Tc(VII) reductase. The role of cytochromec 3 in the mechanism is also discussed.

[5] Nickel-iron hydrogenase

1994 ◽  
pp. 43-68 ◽  
Author(s):  
Richard Cammack ◽  
Victor M. Fernandez ◽  
E. Claude Hatchikian
Keyword(s):  
Nickel Iron Hydrogenase ◽  
Nickel Iron ◽  
Iron Hydrogenase

scholarly journals E. coli Nickel-Iron Hydrogenase 1 Catalyses Non-native Reduction of Flavins: Demonstration for Alkene Hydrogenation by Old Yellow Enzyme

2020 ◽  
Author(s):  
Shiny Joseph Srinivasan ◽  
Sarah Cleary ◽  
Caroline Paul ◽  
Miguel A. Ramirez ◽  
Kylie Vincent
Keyword(s):  
Escherichia Coli ◽  
Turnover Number ◽  
Old Yellow Enzyme ◽  
Nickel Iron Hydrogenase ◽  
Nickel Iron ◽  
E Coli ◽  
Dependent Activity ◽  
Iron Hydrogenase ◽  
Alkene Hydrogenation ◽  
Total Turnover

<p>Robust [NiFe] hydrogenase 1 (Hyd1) from <i>Escherichia coli</i> is shown to have non-native, H<sub>2</sub>-dependent activity for FMN and FAD reduction, and to function as a promising recycling system for FMNH<sub>2</sub> supply to flavoenzymes for chemical synthesis, giving a total turnover number over 10 million when coupled with an Old Yellow Enzyme ene reductase. </p>

Mechanism of H−H Activation by Nickel−Iron Hydrogenase

1998 ◽  
Vol 120 (3) ◽  
pp. 548-555 ◽  
Author(s):  
Maria Pavlov ◽  
Per E. M. Siegbahn ◽  
Margareta R. A. Blomberg ◽  
Robert H. Crabtree
Keyword(s):  
Nickel Iron Hydrogenase ◽  
Nickel Iron ◽  
Iron Hydrogenase

scholarly journals E. coli Nickel-Iron Hydrogenase 1 Catalyses Non-native Reduction of Flavins: Demonstration for Alkene Hydrogenation by Old Yellow Enzyme

2020 ◽  
Author(s):  
Shiny Joseph Srinivasan ◽  
Sarah Cleary ◽  
Caroline Paul ◽  
Miguel A. Ramirez ◽  
Kylie Vincent
Keyword(s):  
Escherichia Coli ◽  
Turnover Number ◽  
Old Yellow Enzyme ◽  
Nickel Iron Hydrogenase ◽  
Nickel Iron ◽  
E Coli ◽  
Dependent Activity ◽  
Iron Hydrogenase ◽  
Alkene Hydrogenation ◽  
Total Turnover

<p>Robust [NiFe] hydrogenase 1 (Hyd1) from <i>Escherichia coli</i> is shown to have non-native, H<sub>2</sub>-dependent activity for FMN and FAD reduction, and to function as a promising recycling system for FMNH<sub>2</sub> supply to flavoenzymes for chemical synthesis, giving a total turnover number over 10 thousand when coupled with an Old Yellow Enzyme ene reductase. </p>

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