{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T04:19:10Z","timestamp":1776053950171,"version":"3.50.1"},"reference-count":59,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2010,6,15]],"date-time":"2010-06-15T00:00:00Z","timestamp":1276560000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2010,6,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Previous studies have demonstrated that\n            <jats:italic>Geobacter sulfurreducens<\/jats:italic>\n            requires the\n            <jats:italic>c<\/jats:italic>\n            -type cytochrome OmcZ, which is present in large (OmcZ\n            <jats:sub>L<\/jats:sub>\n            ; 50-kDa) and small (OmcZ\n            <jats:sub>S<\/jats:sub>\n            ; 30-kDa) forms, for optimal current production in microbial fuel cells. This protein was further characterized to aid in understanding its role in current production. Subcellular-localization studies suggested that OmcZ\n            <jats:sub>S<\/jats:sub>\n            was the predominant extracellular form of OmcZ. N- and C-terminal amino acid sequence analysis of purified OmcZ\n            <jats:sub>S<\/jats:sub>\n            and molecular weight measurements indicated that OmcZ\n            <jats:sub>S<\/jats:sub>\n            is a cleaved product of OmcZ\n            <jats:sub>L<\/jats:sub>\n            retaining all 8 hemes, including 1 heme with the unusual\n            <jats:italic>c<\/jats:italic>\n            -type heme-binding motif CX\n            <jats:sub>14<\/jats:sub>\n            CH. The purified OmcZ\n            <jats:sub>S<\/jats:sub>\n            was remarkably thermally stable (thermal-denaturing temperature, 94.2\u00b0C). Redox titration analysis revealed that the midpoint reduction potential of OmcZ\n            <jats:sub>S<\/jats:sub>\n            is approximately \u2212220 mV (versus the standard hydrogen electrode [SHE]) with nonequivalent heme groups that cover a large reduction potential range (\u2212420 to \u221260 mV). OmcZ\n            <jats:sub>S<\/jats:sub>\n            transferred electrons\n            <jats:italic>in vitro<\/jats:italic>\n            to a diversity of potential extracellular electron acceptors, such as Fe(III) citrate, U(VI), Cr(VI), Au(III), Mn(IV) oxide, and the humic substance analogue anthraquinone-2,6-disulfonate, but not Fe(III) oxide. The biochemical properties and extracellular localization of OmcZ suggest that it is well suited for promoting electron transfer in current-producing biofilms of\n            <jats:italic>G. sulfurreducens<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/aem.00027-10","type":"journal-article","created":{"date-parts":[[2010,4,17]],"date-time":"2010-04-17T01:47:46Z","timestamp":1271468866000},"page":"3999-4007","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":246,"title":["Purification and Characterization of OmcZ, an Outer-Surface, Octaheme\n            <i>c<\/i>\n            -Type Cytochrome Essential for Optimal Current Production by\n            <i>Geobacter sulfurreducens<\/i>"],"prefix":"10.1128","volume":"76","author":[{"given":"Kengo","family":"Inoue","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003"},{"name":"Interdisciplinary Research Organization, University of Miyazaki, Miyazaki, Japan"}]},{"given":"Xinlei","family":"Qian","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003"}]},{"given":"Leonor","family":"Morgado","sequence":"additional","affiliation":[{"name":"Requimte-CQFB, Departamento Qui\u0301mica, Faculdade de Cie\u0302ncias e Tecnologia, Universidade Nova de Lisboa, Campus Caparica, Portugal"}]},{"given":"Byoung-Chan","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003"}]},{"given":"Tu\u0308nde","family":"Mester","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003"}]},{"given":"Mounir","family":"Izallalen","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of 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