{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,12]],"date-time":"2026-07-12T05:07:41Z","timestamp":1783832861504,"version":"3.55.0"},"reference-count":36,"publisher":"Wiley","issue":"26","license":[{"start":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T00:00:00Z","timestamp":1777248000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T00:00:00Z","timestamp":1777248000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100000646","name":"Japan Society for the Promotion of Science London","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000646","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Chemistry A European J"],"published-print":{"date-parts":[[2026,7,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    PM0042 from\u00a0\n                    <jats:italic>Pasteurella multocida<\/jats:italic>\n                    \u00a0is a heme\u2010degrading enzyme homologous to HutZ from\u00a0\n                    <jats:italic>Vibrio cholerae<\/jats:italic>\n                    , but uniquely contains a glycine\u2013histidine (GH) repeat motif at its C\u2010terminal region. Unlike HutZ, PM0042 exhibits a threefold increase in heme degradation activity upon Fe\n                    <jats:sup>2+<\/jats:sup>\n                    addition, yet the underlying mechanism has remained unclear. Here, we investigated the effect of Fe\n                    <jats:sup>2+<\/jats:sup>\n                    on the catalytic process of PM0042. Spectroscopic analyses revealed that Fe\n                    <jats:sup>2<\/jats:sup>\n                    <jats:sup>+<\/jats:sup>\n                    binding does not induce structural changes at either distal or proximal heme sites. Kinetic studies of individual steps in the degradation pathway demonstrated that the reduction of ferric heme to ferrous heme is the rate\u2010determining step and is markedly accelerated by Fe\n                    <jats:sup>2+<\/jats:sup>\n                    . Other steps, including O\n                    <jats:sub>2<\/jats:sub>\n                    binding, verdoheme formation, and biliverdin production, were unaffected. Mutational analysis introducing a His\u2010rich motif into HutZ confirmed that Fe\n                    <jats:sup>2+<\/jats:sup>\n                    enhances activity when bound near the proximal site. These findings suggest that Fe\n                    <jats:sup>2+<\/jats:sup>\n                    acts as an electron mediator rather than a structural modulator, facilitating electron transfer from reductant to heme iron. This study provides mechanistic insight into metal\u2010assisted catalysis in bacterial heme degradation and highlights the functional role of GH repeat sequences in electron transfer.\n                  <\/jats:p>","DOI":"10.1002\/chem.71078","type":"journal-article","created":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T06:32:26Z","timestamp":1777357946000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Mechanism of Enhancement by the Fe\n                    <sup>2+<\/sup>\n                    \u2010Induced Heme Degradation Activity of PM0042 From\n                    <i>Pasteurella multocida<\/i>"],"prefix":"10.1002","volume":"32","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9270-8329","authenticated-orcid":false,"given":"Takeshi","family":"Uchida","sequence":"first","affiliation":[{"name":"Department of Chemistry, Faculty of Science Hokkaido University  Sapporo Japan"},{"name":"Graduate School of Chemical Sciences and Engineering Hokkaido University  Sapporo Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akinobu","family":"Tatsumi","sequence":"additional","affiliation":[{"name":"Graduate School of Chemical Sciences and Engineering Hokkaido University  Sapporo Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5868-0462","authenticated-orcid":false,"given":"Koichiro","family":"Ishimori","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Science Hokkaido University  Sapporo Japan"},{"name":"Graduate School of Chemical Sciences and Engineering Hokkaido University  Sapporo 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