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Evolution of quinol oxidation within the heme-copper oxidoreductase superfamily

Murali, Ranjani and Hemp, James and Gennis, Robert B. (2022) Evolution of quinol oxidation within the heme-copper oxidoreductase superfamily. Biochimica et Biophysica Acta, 1863 (8). Art. No. 148907. ISSN 0005-2728. doi:10.1016/j.bbabio.2022.148907.

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The heme‑copper oxidoreductase (HCO) superfamily is a large superfamily of terminal respiratory enzymes that are widely distributed across the three domains of life. The superfamily includes biochemically diverse oxygen reductases and nitric oxide reductases that are pivotal in the pathways of aerobic respiration and denitrification. The adaptation of HCOs to use quinol as the electron donor instead of cytochrome c has significant implication for the respiratory flexibility and energetic efficiency of the respiratory chains that include them. In this work, we explore the adaptation of this scaffold to two different electron donors, cytochromes c and quinols, with extensive sequence analysis of these enzymes from publicly available datasets. Our work shows that quinol oxidation evolved independently within the HCO superfamily at least seven times. Enzymes from only two of these independently evolved clades have been biochemically well-characterized. Combining structural modeling with sequence analysis, we identify putative quinol binding sites in each of the novel quinol oxidases. Our analysis of experimental and modeling data suggests that the quinol binding site appears to have evolved at the same structural position within the scaffold more than once.

Item Type:Article
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URLURL TypeDescription
Murali, Ranjani0000-0003-4073-9910
Hemp, James0000-0001-7193-0553
Gennis, Robert B.0000-0002-3805-6945
Additional Information:We wish to thank the following for funding: National Institutes of Health R01 AI148160 (to R.B.G.). We thank Dr. Dan Utter for his help with implementation of Alphafold for structural model generation.
Funding AgencyGrant Number
NIHR01 AI148160
Issue or Number:8
Record Number:CaltechAUTHORS:20221014-968413500.6
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:117415
Deposited By: Research Services Depository
Deposited On:18 Oct 2022 22:07
Last Modified:18 Oct 2022 22:07

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