Second and outer coordination sphere effects in nitrogenase, hydrogenase, formate dehydrogenase, and CO dehydrogenase

ST Stripp, BR Duffus, V Fourmond, C Léger… - Chemical …, 2022 - ACS Publications
Gases like H2, N2, CO2, and CO are increasingly recognized as critical feedstock in “green”
energy conversion and as sources of nitrogen and carbon for the agricultural and chemical …

[FeFe]-Hydrogenases: maturation and reactivity of enzymatic systems and overview of biomimetic models

JT Kleinhaus, F Wittkamp, S Yadav… - Chemical Society …, 2021 - pubs.rsc.org
While hydrogen plays an ever-increasing role in modern society, nature has utilized
hydrogen since a very long time as an energy carrier and storage molecule. Among the …

Biochemical and artificial pathways for the reduction of carbon dioxide, nitrite and the competing proton reduction: effect of 2 nd sphere interactions in catalysis

S Amanullah, P Saha, A Nayek, ME Ahmed… - Chemical Society …, 2021 - pubs.rsc.org
Reduction of oxides and oxoanions of carbon and nitrogen are of great contemporary
importance as they are crucial for a sustainable environment. Substantial research has been …

The catalytic cycle of [FeFe] hydrogenase: A tale of two sites

JA Birrell, P Rodriguez-Macia, EJ Reijerse… - Coordination Chemistry …, 2021 - Elsevier
Ever since the discovery of hydrogenases over 90 years ago (Stephenson and Stickland,
1931), their structure and mechanism of action have been intensively investigated. Of the …

Current state of [FeFe]-hydrogenase research: biodiversity and spectroscopic investigations

H Land, M Senger, G Berggren, ST Stripp - ACS catalysis, 2020 - ACS Publications
Hydrogenases are redox enzymes that catalyze the conversion of protons and molecular
hydrogen (H2). Based on the composition of the active site cofactor, the monometallic [Fe] …

Kinetic modeling of the reversible or irreversible electrochemical responses of FeFe-hydrogenases

A Fasano, C Baffert, C Schumann… - Journal of the …, 2024 - ACS Publications
The enzyme FeFe-hydrogenase catalyzes H2 evolution and oxidation at an active site that
consists of a [4Fe-4S] cluster bridged to a [Fe2 (CO) 3 (CN) 2 (azadithiolate)] subsite …

Spectroscopic and computational evidence that [FeFe] hydrogenases operate exclusively with CO-bridged intermediates

JA Birrell, V Pelmenschikov, N Mishra… - Journal of the …, 2019 - ACS Publications
[FeFe] hydrogenases are extremely active H2-converting enzymes. Their mechanism
remains highly controversial, in particular, the nature of the one-electron and two-electron …

The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases

O Lampret, J Duan, E Hofmann… - Proceedings of the …, 2020 - National Acad Sciences
As paradigms for proton-coupled electron transfer in enzymes and benchmarks for a fully
renewable H2 technology,[FeFe]-hydrogenases behave as highly reversible electrocatalysts …

Proton transfer mechanisms in bimetallic hydrogenases

H Tai, S Hirota, ST Stripp - Accounts of Chemical Research, 2020 - ACS Publications
Conspectus Hydrogenases are metalloenzymes that catalyze proton reduction and H2
oxidation with outstanding efficiency. They are model systems for bioinorganic chemistry …

Tuning catalytic bias of hydrogen gas producing hydrogenases

JH Artz, OA Zadvornyy, DW Mulder… - Journal of the …, 2019 - ACS Publications
Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas
oxidation catalysis. The interactions of the iron–sulfur-containing catalytic site with the local …