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The unusual formaldehyde-induced activation of [NiFe]-hydrogenase: Implications from protein film electrochemistry and infrared spectroscopy.

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Názov: The unusual formaldehyde-induced activation of [NiFe]-hydrogenase: Implications from protein film electrochemistry and infrared spectroscopy.
Autori: Wan L; Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany; State Key Laboratory of Medicinal Chemical Biology, College of Life Science, Nankai University, Tianjin, 300350, China; Nankai International Advanced Research Institute (Futian), Nankai University, Shenzhen, Guangdong, 518045, China., Gao Y; Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany; State Key Laboratory of Medicinal Chemical Biology, College of Life Science, Nankai University, Tianjin, 300350, China., DeBeer S; Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany., Rüdiger O; Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany. Electronic address: olaf.ruediger@cec.mpg.de.
Zdroj: Bioelectrochemistry (Amsterdam, Netherlands) [Bioelectrochemistry] 2025 Oct; Vol. 165, pp. 108974. Date of Electronic Publication: 2025 Mar 19.
Spôsob vydávania: Journal Article
Jazyk: English
Informácie o časopise: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 100953583 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1878-562X (Electronic) Linking ISSN: 15675394 NLM ISO Abbreviation: Bioelectrochemistry Subsets: MEDLINE
Imprint Name(s): Original Publication: [Amsterdam?] : Elsevier, 2000-
Výrazy zo slovníka MeSH: Hydrogenase*/metabolism , Hydrogenase*/chemistry , Hydrogenase*/antagonists & inhibitors , Formaldehyde*/pharmacology, Escherichia coli/enzymology ; Enzyme Activation/drug effects ; Hydrogen-Ion Concentration ; Electrochemical Techniques ; Oxidation-Reduction ; Hydrogen/metabolism ; Electrochemistry ; Spectrophotometry, Infrared ; Spectroscopy, Fourier Transform Infrared
Abstrakt: Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests:Yanxin Gao reports financial support was provided by China Scholarship Council. Lei Wan reports financial support was provided by Alexander von Humboldt Foundation. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Here we investigate how formaldehyde (HCHO), a known strong inhibitor of [FeFe]‑hydrogenases and a mild inhibitor of [NiFe]‑hydrogenases, may exert more complex effects on this group of metalloenzymes, which reversibly catalyze the 2H + /H₂ reaction. We investigated the [NiFe]‑hydrogenase Hyd-2 from E. coli using protein film electrochemistry, a technique that enables the measurement of enzyme activity when the enzyme is adequately adsorbed on the electrode. The effect of HCHO on the electrocatalytic performance of Hyd-2 is highly dependent on the buffer pH and the direction of catalysis. During H₂ production, HCHO consistently acts as an inhibitor of Hyd-2. However, this effect is reversed in acidic pH values, where HCHO can mildly enhance the electrocatalytic H₂ oxidation by Hyd-2. FTIR investigations did not detect any new redox intermediate resulting from the inhibition or activation. Therefore, we propose that HCHO - a natural electrophile that can readily react with nucleophiles and proton acceptors - may facilitate the transfer protons during the rapid transformation of different redox species participating in the catalytic cycle of [NiFe]‑hydrogenases.
(Copyright © 2024. Published by Elsevier B.V.)
Substance Nomenclature: EC 1.12.7.2 (Hydrogenase)
1HG84L3525 (Formaldehyde)
EC 1.12.- (nickel-iron hydrogenase)
7YNJ3PO35Z (Hydrogen)
Entry Date(s): Date Created: 20250327 Date Completed: 20250607 Latest Revision: 20250607
Update Code: 20250608
DOI: 10.1016/j.bioelechem.2025.108974
PMID: 40147361
Databáza: MEDLINE
Popis
Abstrakt:Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests:Yanxin Gao reports financial support was provided by China Scholarship Council. Lei Wan reports financial support was provided by Alexander von Humboldt Foundation. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br />Here we investigate how formaldehyde (HCHO), a known strong inhibitor of [FeFe]‑hydrogenases and a mild inhibitor of [NiFe]‑hydrogenases, may exert more complex effects on this group of metalloenzymes, which reversibly catalyze the 2H <sup>+</sup> /H₂ reaction. We investigated the [NiFe]‑hydrogenase Hyd-2 from E. coli using protein film electrochemistry, a technique that enables the measurement of enzyme activity when the enzyme is adequately adsorbed on the electrode. The effect of HCHO on the electrocatalytic performance of Hyd-2 is highly dependent on the buffer pH and the direction of catalysis. During H₂ production, HCHO consistently acts as an inhibitor of Hyd-2. However, this effect is reversed in acidic pH values, where HCHO can mildly enhance the electrocatalytic H₂ oxidation by Hyd-2. FTIR investigations did not detect any new redox intermediate resulting from the inhibition or activation. Therefore, we propose that HCHO - a natural electrophile that can readily react with nucleophiles and proton acceptors - may facilitate the transfer protons during the rapid transformation of different redox species participating in the catalytic cycle of [NiFe]‑hydrogenases.<br /> (Copyright © 2024. Published by Elsevier B.V.)
ISSN:1878-562X
DOI:10.1016/j.bioelechem.2025.108974