{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T20:44:25Z","timestamp":1792010665356,"version":"4.4.0"},"reference-count":349,"publisher":"SAGE Publications","issue":"16","license":[{"start":{"date-parts":[[2021,5,10]],"date-time":"2021-05-10T00:00:00Z","timestamp":1620604800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2021,5,10]],"date-time":"2021-05-10T00:00:00Z","timestamp":1620604800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Antioxidants &amp; Redox Signaling"],"published-print":{"date-parts":[[2021,6]]},"abstract":"<jats:sec>\n                    <jats:title>Significance:<\/jats:title>\n                    <jats:p>\n                      Cytochrome\n                      <jats:italic toggle=\"yes\">bd<\/jats:italic>\n                      is a ubiquinol:oxygen oxidoreductase of many prokaryotic respiratory chains with a unique structure and functional characteristics. Its primary role is to couple the reduction of molecular oxygen, even at submicromolar concentrations, to water with the generation of a proton motive force used for adenosine triphosphate production. Cytochrome\n                      <jats:italic toggle=\"yes\">bd<\/jats:italic>\n                      is found in many bacterial pathogens and, surprisingly, in bacteria formally denoted as anaerobes. It endows bacteria with resistance to various stressors and is a potential drug target.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Recent Advances:<\/jats:title>\n                    <jats:p>\n                      We summarize recent advances in the biochemistry, structure, and physiological functions of cytochrome\n                      <jats:italic toggle=\"yes\">bd<\/jats:italic>\n                      in the light of exciting new three-dimensional structures of the oxidase. The newly discovered roles of cytochrome\n                      <jats:italic toggle=\"yes\">bd<\/jats:italic>\n                      in contributing to bacterial protection against hydrogen peroxide, nitric oxide, peroxynitrite, and hydrogen sulfide are assessed.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Critical Issues:<\/jats:title>\n                    <jats:p>Fundamental questions remain regarding the precise delineation of electron flow within this multihaem oxidase and how the extraordinarily high affinity for oxygen is accomplished, while endowing bacteria with resistance to other small ligands.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Future Directions:<\/jats:title>\n                    <jats:p>\n                      It is clear that cytochrome\n                      <jats:italic toggle=\"yes\">bd<\/jats:italic>\n                      is unique in its ability to confer resistance to toxic small molecules, a property that is significant for understanding the propensity of pathogens to possess this oxidase. Since cytochrome\n                      <jats:italic toggle=\"yes\">bd<\/jats:italic>\n                      is a uniquely bacterial enzyme, future research should focus on harnessing fundamental knowledge of its structure and function to the development of novel and effective antibacterial agents.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1089\/ars.2020.8039","type":"journal-article","created":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T02:17:24Z","timestamp":1600049844000},"page":"1280-1318","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":130,"title":["Bacterial Oxidases of the Cytochrome\n                    <i>bd<\/i>\n                    Family: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets"],"prefix":"10.1177","volume":"34","author":[{"given":"Vitaliy B.","family":"Borisov","sequence":"first","affiliation":[{"name":"Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russian Federation."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey A.","family":"Siletsky","sequence":"additional","affiliation":[{"name":"Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russian Federation."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessandro","family":"Paiardini","sequence":"additional","affiliation":[{"name":"Department of Biochemical Sciences, Sapienza University of Rome, Rome, Italy."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Hoogewijs","sequence":"additional","affiliation":[{"name":"Department of Medicine\/Physiology, University of Fribourg, Fribourg, Switzerland."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena","family":"Forte","sequence":"additional","affiliation":[{"name":"Department of Biochemical Sciences, Sapienza University of Rome, 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