Bioassembly of complex iron–sulfur enzymes: hydrogenases and nitrogenases

RD Britt, G Rao, L Tao - Nature Reviews Chemistry, 2020 - nature.com
Nature uses multinuclear metal clusters to catalyse a number of important multielectron
redox reactions. Examples that employ complex Fe–S clusters in catalysis include the Fe …

Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe–S maturase proteins HydE, HydF, and HydG

RD Britt, G Rao, L Tao - Chemical science, 2020 - pubs.rsc.org
[FeFe] hydrogenases carry out the redox interconversion of protons and molecular hydrogen
(2H++ 2e−⇌ H2) at a complex Fe–S active site known as the H-cluster. The H-cluster …

Mimicking the electron transport chain and active site of [FeFe] hydrogenases in one metal–organic framework: factors that influence charge transport

AT Castner, BA Johnson, SM Cohen… - Journal of the American …, 2021 - ACS Publications
[FeFe] hydrogenase (H2ase) enzymes are effective proton reduction catalysts capable of
forming molecular dihydrogen with a high turnover frequency at low overpotential. The …

Radical SAM enzyme HydE generates adenosylated Fe (I) intermediates en route to the [FeFe]-hydrogenase catalytic H-cluster

L Tao, SA Pattenaude, S Joshi, TP Begley… - Journal of the …, 2020 - ACS Publications
The H-cluster of [FeFe]-hydrogenase consists of a [4Fe–4S] H-subcluster linked by a
cysteinyl bridge to a unique organometallic [2Fe] H-subcluster assigned as the site of …

Fully Refined Semisynthesis of the [FeFe] Hydrogenase H-Cluster

G Rao, X Yu, Y Zhang, TB Rauchfuss, RD Britt - Biochemistry, 2023 - ACS Publications
[FeFe] hydrogenases contain a 6-Fe cofactor that serves as the active site for efficient redox
interconversion between H2 and protons. The biosynthesis of the so-called H-cluster …

Stepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamics

M Senger, S Mebs, J Duan… - Proceedings of the …, 2016 - National Acad Sciences
The six-iron cofactor of [FeFe]-hydrogenases (H-cluster) is the most efficient H2-forming
catalyst in nature. It comprises a diiron active site with three carbon monoxide (CO) and two …

Evidence of Atypical Structural Flexibility of the Active Site Surrounding of an [FeFe] Hydrogenase from Clostridium beijerinkii

PS Corrigan, SH Majer, A Silakov - Journal of the American …, 2023 - ACS Publications
[FeFe] hydrogenase from Clostridium beijerinkii (Cb HydA1) is an unusual hydrogenase in
that it can withstand prolonged exposure to O2 by reversibly converting into an O2 …

Organometallic Fe2(μ-SH)2(CO)4(CN)2 Cluster Allows the Biosynthesis of the [FeFe]-Hydrogenase with Only the HydF Maturase

Y Zhang, L Tao, TJ Woods, RD Britt… - Journal of the …, 2022 - ACS Publications
The biosynthesis of the active site of the [FeFe]-hydrogenases (HydA1), the H-cluster, is of
interest because these enzymes are highly efficient catalysts for the oxidation and …

A personal account on 25 years of scientific literature on [FeFe]-hydrogenase

JW Sidabras, ST Stripp - JBIC Journal of Biological Inorganic Chemistry, 2023 - Springer
Abstract [FeFe]-hydrogenases are gas-processing metalloenzymes that catalyze H2
oxidation and proton reduction (H2 release) in microorganisms. Their high turnover …

From enzyme maturation to synthetic chemistry: the case of hydrogenases

V Artero, G Berggren, M Atta, G Caserta… - Accounts of Chemical …, 2015 - ACS Publications
Conspectus Water splitting into oxygen and hydrogen is one of the most attractive strategies
for storing solar energy and electricity. Because the processes at work are multielectronic …