{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T02:15:49Z","timestamp":1791684949419,"version":"4.3.4"},"reference-count":42,"publisher":"National Academy of Sciences","issue":"24","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2013,6,11]]},"abstract":"<jats:p>\n                    The diheme enzyme MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate a tryptophan tryptophylquinone cofactor. The MauG-catalyzed reaction proceeds via a\n                    <jats:italic>bis<\/jats:italic>\n                    -Fe(IV) intermediate in which one heme is present as Fe(IV)=O and the other as Fe(IV) with axial histidine and tyrosine ligation. Herein, a unique near-infrared absorption feature exhibited specifically in\n                    <jats:italic>bis<\/jats:italic>\n                    -Fe(IV) MauG is described, and evidence is presented that it results from a charge-resonance-transition phenomenon. As the two hemes are physically separated by 14.5 \u00c5, a hole-hopping mechanism is proposed in which a tryptophan residue located between the hemes is reversibly oxidized and reduced to increase the effective electronic coupling element and enhance the rate of reversible electron transfer between the hemes in\n                    <jats:italic>bis<\/jats:italic>\n                    -Fe(IV) MauG. Analysis of the MauG structure reveals that electron transfer via this mechanism is rapid enough to enable a charge-resonance stabilization of the\n                    <jats:italic>bis<\/jats:italic>\n                    -Fe(IV) state without direct contact between the hemes. The finding of the charge-resonance-transition phenomenon explains why the\n                    <jats:italic>bis<\/jats:italic>\n                    -Fe(IV) intermediate is stabilized in MauG and does not permanently oxidize its own aromatic residues.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1301544110","type":"journal-article","created":{"date-parts":[[2013,5,30]],"date-time":"2013-05-30T01:03:13Z","timestamp":1369875793000},"page":"9639-9644","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":70,"title":["Tryptophan-mediated charge-resonance stabilization in the\n                    <i>bis<\/i>\n                    -Fe(IV) redox state of MauG"],"prefix":"10.1073","volume":"110","author":[{"given":"Jiafeng","family":"Geng","sequence":"first","affiliation":[{"name":"Department of Chemistry, Center for Diagnostics and Therapeutics, and Molecular Basis of Disease Program, Georgia State University, Atlanta, GA 30303; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kednerlin","family":"Dornevil","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Center for Diagnostics and Therapeutics, and Molecular Basis of Disease Program, Georgia State University, Atlanta, GA 30303; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor L.","family":"Davidson","sequence":"additional","affiliation":[{"name":"Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL 32827"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aimin","family":"Liu","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Center for Diagnostics and Therapeutics, and Molecular Basis of Disease Program, Georgia State University, Atlanta, GA 30303; 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