Search: onr:"swepub:oai:DiVA.org:su-215986" >
Molecular Basis of ...
Molecular Basis of the Electron Bifurcation Mechanism in the [FeFe]- Hydrogenase Complex HydABC
-
Katsyv, Alexander. (author)
-
Kumar, Anuj (author)
-
- Saura, Patricia (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
show more...
-
- Pöverlein, Maximilian C. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
Freibert, Sven A. (author)
-
Stripp, Sven T. (author)
-
Jain, Surbhi (author)
-
- Gamiz-Hernandez, Ana P. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Kaila, Ville R. I. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
Müller, Volker (author)
-
Schuller, Jan M. (author)
-
show less...
-
(creator_code:org_t)
- 2023-02-22
- 2023
- English.
-
In: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 145:10, s. 5696-5709
- Related links:
-
https://doi.org/10.1...
-
show more...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- Electron bifurcation is a fundamental energy coupling mechanism widespread in microorganisms that thrive under anoxic conditions. These organisms employ hydrogen to reduce CO2, but the molecular mechanisms have remained enigmatic. The key enzyme responsible for powering these thermodynamically challenging reactions is the electron-bifurcating [FeFe]-hydrogenase HydABC that reduces low-potential ferredoxins (Fd) by oxidizing hydrogen gas (H2). By combining single-particle cryo-electron microscopy (cryoEM) under catalytic turnover conditions with site-directed mutagenesis experiments, functional studies, infrared spectroscopy, and molecular simulations, we show that HydABC from the acetogenic bacteria Acetobacterium woodii and Thermoanaerobacter kivui employ a single flavin mononucleotide (FMN) cofactor to establish electron transfer pathways to the NAD(P)+ and Fd reduction sites by a mechanism that is fundamentally different from classical flavin-based electron bifurcation enzymes. By modulation of the NAD(P)+ binding affinity via reduction of a nearby iron–sulfur cluster, HydABC switches between the exergonic NAD(P)+ reduction and endergonic Fd reduction modes. Our combined findings suggest that the conformational dynamics establish a redox-driven kinetic gate that prevents the backflow of the electrons from the Fd reduction branch toward the FMN site, providing a basis for understanding general mechanistic principles of electron-bifurcating hydrogenases.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Katsyv, Alexande ...
-
Kumar, Anuj
-
Saura, Patricia
-
Pöverlein, Maxim ...
-
Freibert, Sven A ...
-
Stripp, Sven T.
-
show more...
-
Jain, Surbhi
-
Gamiz-Hernandez, ...
-
Kaila, Ville R. ...
-
Müller, Volker
-
Schuller, Jan M.
-
show less...
- About the subject
-
- NATURAL SCIENCES
-
NATURAL SCIENCES
-
and Chemical Science ...
- Articles in the publication
-
Journal of the A ...
- By the university
-
Stockholm University