{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T22:32:20Z","timestamp":1767911540312,"version":"3.49.0"},"reference-count":41,"publisher":"Proceedings of the National Academy of Sciences","issue":"21","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2009,5,26]]},"abstract":"<jats:p>\n            The cofactor composition and electron-transfer kinetics of the reaction center (RC) from a magnesium chelatase (\n            <jats:italic>bchD<\/jats:italic>\n            ) mutant of\n            <jats:italic>Rhodobacter sphaeroides<\/jats:italic>\n            were characterized. In this RC, the special pair (P) and accessory (B) bacteriochlorophyll (BChl) -binding sites contain Zn-BChl rather than BChl\n            <jats:italic>a<\/jats:italic>\n            . Spectroscopic measurements reveal that Zn-BChl also occupies the H sites that are normally occupied by bacteriopheophytin in wild type, and at least 1 of these Zn-BChl molecules is involved in electron transfer in intact Zn-RCs with an efficiency of &gt;95% of the wild-type RC. The absorption spectrum of this Zn-containing RC in the near-infrared region associated with P and B is shifted from 865 to 855 nm and from 802 to 794 nm respectively, compared with wild type. The bands of P and B in the visible region are centered at 600 nm, similar to those of wild type, whereas the H-cofactors have a band at 560 nm, which is a spectral signature of monomeric Zn-BChl in organic solvent. The Zn-BChl H-cofactor spectral differences compared with the P and B positions in the visible region are proposed to be due to a difference in the 5th ligand coordinating the Zn. We suggest that this coordination is a key feature of protein\u2013cofactor interactions, which significantly contributes to the redox midpoint potential of H and the formation of the charge-separated state, and provides a unifying explanation for the properties of the primary acceptor in photosystems I (PS1) and II (PS2).\n          <\/jats:p>","DOI":"10.1073\/pnas.0812719106","type":"journal-article","created":{"date-parts":[[2009,5,14]],"date-time":"2009-05-14T01:10:29Z","timestamp":1242263429000},"page":"8537-8542","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":23,"title":["Electron transfer in the\n            <i>Rhodobacter sphaeroides<\/i>\n            reaction center assembled with zinc bacteriochlorophyll"],"prefix":"10.1073","volume":"106","author":[{"given":"Su","family":"Lin","sequence":"first","affiliation":[{"name":"The Biodesign Institute at Arizona State University, Arizona State University, Tempe, AZ 85287-5201;"},{"name":"Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604;"}]},{"given":"Paul R.","family":"Jaschke","sequence":"additional","affiliation":[{"name":"Departments of cMicrobiology and Immunology and"}]},{"given":"Haiyu","family":"Wang","sequence":"additional","affiliation":[{"name":"The Biodesign Institute at Arizona State University, Arizona State University, Tempe, AZ 85287-5201;"}]},{"given":"Mark","family":"Paddock","sequence":"additional","affiliation":[{"name":"Department of Physics, University of California at San Diego, La Jolla, CA 92093"}]},{"given":"Aaron","family":"Tufts","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604;"}]},{"given":"James P.","family":"Allen","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604;"}]},{"given":"Federico I.","family":"Rosell","sequence":"additional","affiliation":[{"name":"Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, Canada V6T 1Z3; and"}]},{"given":"A. Grant","family":"Mauk","sequence":"additional","affiliation":[{"name":"Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, Canada V6T 1Z3; and"}]},{"given":"Neal W.","family":"Woodbury","sequence":"additional","affiliation":[{"name":"The Biodesign Institute at Arizona State University, Arizona State University, Tempe, AZ 85287-5201;"},{"name":"Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604;"}]},{"given":"J. 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