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This single mutation induces a change of heme coordination state and bonding character which change carbon monoxide (CO) and nitric oxide (NO) dynamics. In H93C Mb the increased Fe<jats:sup>2+<\/jats:sup>\u2013S distance weakens this bond which is replaced with a distal Fe<jats:sup>2+<\/jats:sup>\u2013His64 ligation. We measured dynamics very different from wild type Mb but similar with those measured in soluble guanylate cyclase (sGC). Whereas NO induces a direct negative <jats:italic>trans<\/jats:italic> effect, the strain on His64 ligation is sufficient to counteract the positive <jats:italic>trans<\/jats:italic> effect due to CO. After photodissociation, geminate recombination of NO to the transient 4\u2010coordinate heme of H93C occurred with a fast time constant (6.9\u2009ps) identical to that in sGC. Remarkably, we also observed picosecond geminate rebinding of CO to H93C Mb, similarly with sGC in the simultaneous presence of CO and an allosteric stimulator. This CO rebinding dynamics to the 4c\u2010heme in H93C Mb was never measured in other Mb mutants and demonstrates the existence of 5\u2010coordinate heme with CO, explaining the synergistic activation of sGC in presence of CO and a stimulator.<\/jats:p>","DOI":"10.1002\/pro.5231","type":"journal-article","created":{"date-parts":[[2024,11,22]],"date-time":"2024-11-22T14:04:32Z","timestamp":1732284272000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Controlling the <i>trans<\/i> effect induced by nitric oxide and carbon monoxide: <scp>H93C<\/scp> myoglobin versus H\u2010<scp>NOX<\/scp> sensors and soluble guanylate cyclase"],"prefix":"10.1002","volume":"33","author":[{"given":"Byung\u2010Kuk","family":"Yoo","sequence":"first","affiliation":[{"name":"Laboratoire d'Optique et Biosciences, INSERM U\u20101182, CNRS UMR 7645 Ecole Polytechnique  Palaiseau 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