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Conformational coup...
Conformational coupling between the active site and residues within the K-C-channel of the Vibrio cholerae cbb(3)-type (C-family) oxygen reductase
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Ahn, Young O. (author)
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Mahinthichaichan, Paween (author)
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- Lee, Hyun Ju (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Ouyang, Hanlin (author)
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Kaluka, Daniel (author)
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Yeh, Syun-Ru (author)
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- Arjona, Davinia (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Rousseau, Denis L. (author)
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Tajkhorshid, Emad (author)
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- Ädelroth, Pia (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Gennis, Robert B. (author)
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(creator_code:org_t)
- 2014-10-06
- 2014
- English.
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In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 111:42, s. E4419-E4428
- Related links:
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https://www.pnas.org...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- The respiratory chains of nearly all aerobic organisms are terminated by proton-pumping heme-copper oxygen reductases (HCOs). Previous studies have established that C-family HCOs contain a single channel for uptake from the bacterial cytoplasm of all chemical and pumped protons, and that the entrance of the K-C-channel is a conserved glutamate in subunit III. However, the majority of the K-C-channel is within subunit I, and the pathway from this conserved glutamate to subunit I is not evident. In the present study, molecular dynamics simulations were used to characterize a chain of water molecules leading from the cytoplasmic solution, passing the conserved glutamate in subunit III and extending into subunit I. Formation of the water chain, which controls the delivery of protons to the K-C-channel, was found to depend on the conformation of Y241(Vc), located in subunit I at the interface with subunit III. Mutations of Y241(Vc) (to A/F/H/S) in the Vibrio cholerae cbb(3) eliminate catalytic activity, but also cause perturbations that propagate over a 28-angstrom distance to the active site heme b(3). The data suggest a linkage between residues lining the KC-channel and the active site of the enzyme, possibly mediated by transmembrane helix alpha 7, which contains both Y241(Vc) and the active site crosslinked Y255(Vc), as well as two Cu-B histidine ligands. Other mutations of residues within or near helix alpha 7 also perturb the active site, indicating that this helix is involved in modulation of the active site of the enzyme.
Subject headings
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- oxygen reductase
- proton pathway
- bioenergetics
- Vibrio cholerae
- cbb(3)
Publication and Content Type
- ref (subject category)
- art (subject category)
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Ahn, Young O.
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Mahinthichaichan ...
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Lee, Hyun Ju
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Ouyang, Hanlin
-
Kaluka, Daniel
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Yeh, Syun-Ru
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show more...
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Arjona, Davinia
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Rousseau, Denis ...
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Tajkhorshid, Ema ...
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Ädelroth, Pia
-
Gennis, Robert B ...
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biophysics
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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Proceedings of t ...
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Stockholm University