ArticleBiochemistry2006
Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 70 citations in OpenAlex.
- The role of cytochrome oxidases in bacterial virulence.Infection and immunity · 2026Review
- Cytochrome oxidase requirements in Bordetella reveal insights into evolution towards life in the mammalian respiratory tract.PLoS pathogens · 2024Article
- Diversity and evolution of nitric oxide reduction in bacteria and archaea.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- The Redox-Active Tyrosine Is Essential for Proton Pumping in Cytochrome c Oxidase.Frontiers in chemistry · 2021Article
- Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in CytochromeJournal of the American Chemical Society · 2019Article
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Biochemistry · 2018Review
- Oxygen Activation and Energy Conservation by Cytochrome c Oxidase.Chemical reviews · 2018Review
- A Systematic DFT Approach for Studying Mechanisms of Redox Active Enzymes.Frontiers in chemistry · 2018Article
- Activation of dioxygen by copper metalloproteins and insights from model complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.Israel journal of chemistry · 2016Article
- Respiratory Kinetics of Marine Bacteria Exposed to Decreasing Oxygen Concentrations.Applied and environmental microbiology · 2015Article
- The evolution of respiratory O2/NO reductases: an out-of-the-phylogenetic-box perspective.Journal of the Royal Society, Interface · 2014Review
- The K(C) channel in the cbb3-type respiratory oxygen reductase from Rhodobacter capsulatus is required for both chemical and pumped protons.Journal of bacteriology · 2014Article
- Characterization of the nitric oxide reductase from Thermus thermophilus.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Shallow breathing: bacterial life at low O(2).Nature reviews. Microbiology · 2013Review
- 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
- Mechanistic stoichiometry of proton translocation by cytochrome cbb3.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Significant increase of oxidase activity through the genetic incorporation of a tyrosine-histidine cross-link in a myoglobin model of heme-copper oxidase.Angewandte Chemie (International ed. in English) · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
In the respiratory chains of aerobic organisms, oxygen reductase members of the heme-copper superfamily couple the reduction of O2 to proton pumping, generating an electrochemical gradient. There are three distinct families of heme-copper oxygen reductases: A, B, and C types. The A- and B-type oxygen reductases have an active-site tyrosine that forms a unique cross-linked histidine-tyrosine cofactor. In the C-type oxygen reductases (also called cbb3 oxidases), an analogous active-site tyrosine has recently been predicted by molecular modeling to be located within a different transmembrane helix in comparison to the A- and B-type oxygen reductases. In this work, Fourier-transform mass spectrometry is used to show that the predicted tyrosine forms a histidine-tyrosine cross-linked cofactor in the active site of the C-type oxygen reductases. This is the first known example of the evolutionary migration of a post-translationally modified active-site residue. It also verifies the presence of a unique cofactor in all three families of proton-pumping respiratory oxidases, demonstrating that these enzymes likely share a common reaction mechanism and that the histidine-tyrosine cofactor may be a required component for proton pumping.
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