ArticleBiochemistry2011
Alternative initial proton acceptors for the D pathway of Rhodobacter sphaeroides cytochrome c oxidase.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Evidence of Gas Phase Glucosyl Transfer and Glycation in the CID/HCD-Spectra of S-Glucosylated Peptides.International journal of molecular sciences · 2024Article
- Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Obesity-induced changes in kidney mitochondria and endoplasmic reticulum in the presence or absence of leptin.American journal of physiology. Renal physiology · 2015Article
- Philosophy of voltage-gated proton channels.Journal of the Royal Society, Interface · 2014Review
- Peregrination of the selectivity filter delineates the pore of the human voltage-gated proton channel hHV1.The Journal of general physiology · 2013Article
- Role of aspartate 132 at the orifice of a proton pathway in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structure, function, and assembly of heme centers in mitochondrial respiratory complexes.Biochimica et biophysica acta · 2012Review
- The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidases.Biochimica et biophysica acta · 2012Article
- Subunit III-depleted cytochrome c oxidase provides insight into the process of proton uptake by proteins.Biochimica et biophysica acta · 2012Review
- Expanding the view of proton pumping in cytochrome c oxidase through computer simulation.Biochimica et biophysica acta · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
To characterize protein structures that control proton uptake, we assayed forms of cytochrome c oxidase (CcO) containing a carboxyl or a thiol group in line with the initial, internal waters of the D pathway for proton transfer in the presence and absence of subunit III. Subunit III provides approximately half of the protein surrounding the entry region of the D pathway. The N139D/D132N mutant contains a carboxyl group 6 Å within the D pathway and lacks the normal, surface-exposed proton acceptor, Asp-132. With subunit III, the steady-state activity of this mutant is slow, but once subunit III is removed, its activity is the same as that of wild-type CcO lacking subunit III (∼1800 H+/s). Thus, a carboxyl group∼25% within the pathway enhances proton uptake even though the carboxyl has no direct contact with bulk solvent. Protons from solvent apparently move to internal Asp-139 through a short file of waters, normally blocked by subunit III. Cys-139 also supports rapid steady-state proton uptake, demonstrating that an anion other than a carboxyl can attract and transfer protons into the D pathway. When both Asp-132 and Asp/Cys-139 are present, the removal of subunit III increases CcO activity to rates greater than that of normal CcO because of simultaneous proton uptake by two initial acceptors. The results show how the environment of the initial proton acceptor for the D pathway in these CcO forms dictates the pH range of CcO activity, with implications for the function of Asp-132, the normal proton acceptor.
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