NDLI: Calculated Coupling of Transmembrane Electron and Proton Transfer in Dihemic Quinol:Fumarate Reductase

Content Provider	PubMed Central
Author	Haas, Alexander H. Lancaster, C. Roy D.
Copyright Year	2004
Abstract	The quinol:fumarate reductase of Wolinella succinogenes binds a low- and a high-potential heme b group in its transmembrane subunit C. Both hemes are part of the electron transport chain between the two catalytic sites of this redox enzyme. The oxidation-reduction midpoint potentials of the hemes are well established but their assignment in the structure has not yet been determined. By simulating redox titrations, using continuum electrostatics calculations, it was possible to achieve an unequivocal assignment of the low- and high-potential hemes to the distal and proximal positions in the structure, respectively. Prominent features governing the differences in midpoint potential between the two hemes are the higher loss of reaction field energy for the proximal heme and the stronger destabilization of the oxidized form of the proximal heme due to several buried Arg and Lys residues. According to the so-called “E-pathway hypothesis”, quinol:fumarate reductase has previously been postulated to exhibit a novel coupling of transmembrane electron and proton transfer. Simulation of heme b reduction indicates that the protonation state of the conserved residue Glu C180, predicted to play a key role in this process, indeed depends on the redox state of the hemes. This result clearly supports the E-pathway hypothesis.
Related Links	http://dx.doi.org/10.1529/biophysj.104.042945
Ending Page	4315
Page Count	18
Starting Page	4298
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	6
Volume Number	87
Language	English
Publisher	Biophysical Society
Publisher Date	2004-12-01
Access Restriction	Open
Rights Holder	Biophysical Society
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Experimental support for the “E pathway hypothesis” of coupled transmembrane e– and H+ transfer in dihemic quinol:fumarate reductase

Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis.

Hydrogen-Bonded Networks Along and Bifurcation of the E-Pathway in Quinol:Fumarate Reductase

Experimental support for the “E pathway hypothesis” of coupled transmembrane $e^{–}$ and $H^{+}$ transfer in dihemic quinol:fumarate reductase

The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase.

Electron transport and transmembrane proton transfer in photosynthetic systems of oxygenic type in Silico

Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase.

Plasticity of the Quinone-binding Site of the Complex II Homolog Quinol:Fumarate Reductase

Thermodynamics of electron transfer and its coupling to vectorial processes in biological membranes.

Calculated Coupling of Transmembrane Electron and Proton Transfer in Dihemic Quinol:Fumarate Reductase

Similar Documents

Experimental support for the “E pathway hypothesis” of coupled transmembrane e– and H+ transfer in dihemic quinol:fumarate reductase

Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis.

Hydrogen-Bonded Networks Along and Bifurcation of the E-Pathway in Quinol:Fumarate Reductase

Experimental support for the “E pathway hypothesis” of coupled transmembrane $e^{–}$ and $H^{+}$ transfer in dihemic quinol:fumarate reductase

The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase.

Electron transport and transmembrane proton transfer in photosynthetic systems of oxygenic type in Silico

Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase.

Plasticity of the Quinone-binding Site of the Complex II Homolog Quinol:Fumarate Reductase

Thermodynamics of electron transfer and its coupling to vectorial processes in biological membranes.

Calculated Coupling of Transmembrane Electron and Proton Transfer in Dihemic Quinol:Fumarate Reductase