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This functional mechanism requires control of both the redox state and the protonation state. In the present study, isotope-labeled PpcA was produced and the three-dimensional structure of PpcA in the oxidized form was determined by NMR. This is the first solution structure of a G. sulfurreducens cytochrome in the oxidized state. The comparison of oxidized and reduced structures revealed that the heme I axial ligand geometry changed and there were other significant changes in the segments near heme I. The pH-linked conformational rearrangements observed in the vicinity of the redox-Bohr center, both in the oxidized and reduced structures, constitute the structural basis for the differences observed in the pKa values of the redox-Bohr center, providing insights into the e\u2212\/H+ coupling molecular mechanisms driven by PpcA in G. sulfurreducens.<\/jats:p>","DOI":"10.1042\/bcj20160932","type":"journal-article","created":{"date-parts":[[2016,11,15]],"date-time":"2016-11-15T02:25:27Z","timestamp":1479176727000},"page":"231-246","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["Redox- and pH-linked conformational changes in triheme cytochrome PpcA from <i>Geobacter sulfurreducens<\/i>"],"prefix":"10.1042","volume":"474","author":[{"given":"Leonor","family":"Morgado","sequence":"first","affiliation":[{"name":"UCIBIO, REQUIMTE, Departamento de Qu\u00edmica, Faculdade de Ci\u00eancias e Tecnologia, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal"}]},{"given":"Marta","family":"Bruix","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica F\u00edsica Biol\u00f3gica, Instituto de Qu\u00edmica-F\u00edsica \u2018Rocasolano\u2019, CSIC, Serrano 119, 28006 Madrid, Spain"}]},{"given":"P. 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