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A tryptophan positioned between the two hemes in two out of the three known enzymes to form this state, MauG and MbnH, has been proposed as the dominant pathway for interheme electron transfer. The third enzyme, BthA, instead has a serine at this position. Here, we used site-directed mutagenesis of Trp113 in MbnH to test whether this tryptophan is uniquely required for interheme electron transfer. Computational pathway analysis identified the possibility of an alternative, noncovalent route mediated by Arg283 and a heme propionate with possible electronic coupling comparable to that of the native tryptophan pathway. Consistent with this prediction, only simultaneous disruption of both the tryptophan and propionate-mediated pathways abolished bis-FeIV formation entirely. Moreover, only mutants capable of forming bis-FeIV retained the ability to turnover substrate, directly establishing this high-valent state as the catalytic intermediate responsible for substrate modification. These results demonstrate that an intervening tryptophan is not required for fast interheme electron transfer, and instead reveal an additional, noncovalent pathway that may be a general feature of diheme peroxidases.<\/jats:p>","DOI":"10.1021\/jacs.6c13740","type":"journal-article","created":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T15:01:48Z","timestamp":1791644508000},"page":"45788-45800","source":"Crossref","is-referenced-by-count":0,"title":["Deciphering Interheme\nElectron-Transfer Pathways in\na Diheme Peroxidase from Methane-Oxidizing Bacteria"],"prefix":"10.1021","volume":"148","author":[{"given":"Riley E.","family":"Stein","sequence":"first","affiliation":[{"name":"University of Illinois Urbana\u2212Champaign , , 600 S. Mathews Ave, Chemical and Life Sciences Laboratory , , ,","place":["Urbana, Illinois, United States, 61801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7162-3676","authenticated-orcid":true,"given":"Anastasia C.","family":"Manesis","sequence":"additional","affiliation":[{"name":"University of Illinois Urbana\u2212Champaign , , 600 S. Mathews Ave, Chemical and Life Sciences Laboratory , , ,","place":["Urbana, Illinois, United States, 61801"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,10]]},"reference":[{"issue":"5089","key":"2026102809104437600_cit1","doi-asserted-by":"publisher","first-page":"1748","DOI":"10.1126\/science.1334573","article-title":"Crystal Structure of a Complex Between Electron Transfer Partners,\nCytochrome c Peroxidase and Cytochrome c","volume":"258","author":"Pelletier","year":"1992","journal-title":"Science"},{"issue":"18","key":"2026102809104437600_cit2","doi-asserted-by":"publisher","first-page":"5611","DOI":"10.1021\/bi960260m","article-title":"Internal Electron-Transfer\nReactions in Cytochrome c Oxidase","volume":"35","author":"Brzezinski","year":"1996","journal-title":"Biochemistry"},{"issue":"3","key":"2026102809104437600_cit3","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1038\/73244","article-title":"Nitrous\nOxide Reductase from CuA to CuZ","volume":"7","author":"Rosenzweig","year":"2000","journal-title":"Nat. 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A."},{"issue":"1","key":"2026102809104437600_cit13","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-019-09020-4","article-title":"A Widely Distributed\nDiheme Enzyme from Burkholderia That Displays an Atypically Stable\nBis-Fe(IV) State","volume":"10","author":"Rizzolo","year":"2019","journal-title":"Nat. Commun."},{"key":"2026102809104437600_cit14","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1016\/j.abb.2013.10.004","article-title":"MauG, a Diheme Enzyme\nThat Catalyzes Tryptophan Tryptophylquinone\nBiosynthesis by Remote Catalysis","volume":"544","author":"Shin","year":"2014","journal-title":"Arch. Biochem.\nBiophys."},{"issue":"23","key":"2026102809104437600_cit15","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2100680118","article-title":"Copper\nBinding by a Unique Family of Metalloproteins Is Dependent on Kynurenine\nFormation","volume":"118","author":"Manesis","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. 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Reson."},{"key":"2026102809104437600_cit32","doi-asserted-by":"publisher","DOI":"10.1002\/0471721646","volume-title":"Raman Spectroscopy\nfor Chemical Analysis","author":"McCreery","year":"2000","edition":"1"},{"key":"2026102809104437600_cit33","unstructured":"Kurnikov, I. V.\n          \n          HARLEM. 2000."},{"issue":"24","key":"2026102809104437600_cit34","doi-asserted-by":"publisher","first-page":"9639","DOI":"10.1073\/pnas.1301544110","article-title":"Tryptophan-Mediated\nCharge-Resonance Stabilization in the Bis-Fe(IV) Redox State of MauG","volume":"110","author":"Geng","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"11","key":"2026102809104437600_cit35","doi-asserted-by":"publisher","first-page":"4043","DOI":"10.1021\/ja00037a004","article-title":"Mapping\nElectron Tunneling Pathways:\nAn Algorithm That Finds the \u201cMinimum Length\u201d\/Maximum\nCoupling Pathway between Electron Donors and Acceptors in Proteins","volume":"114","author":"Betts","year":"1992","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026102809104437600_cit36","doi-asserted-by":"publisher","first-page":"722","DOI":"10.1063\/1.458426","article-title":"A Predictive Theoretical\nModel for Electron Tunneling\nPathways in Proteins","volume":"92","author":"Onuchic","year":"1990","journal-title":"J. Chem. Phys."},{"issue":"9","key":"2026102809104437600_cit37","doi-asserted-by":"publisher","first-page":"3640","DOI":"10.1073\/pnas.71.9.3640","article-title":"Electron\nTransfer Between Biological Molecules by Thermally Activated Tunneling","volume":"71","author":"Hopfield","year":"1974","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"12","key":"2026102809104437600_cit38","doi-asserted-by":"publisher","first-page":"4860","DOI":"10.1063\/1.432142","article-title":"Temperature\nDependent Activation Energy for Electron Transfer between Biological\nMolecules","volume":"64","author":"Jortner","year":"1976","journal-title":"J. Chem. Phys."},{"issue":"30","key":"2026102809104437600_cit39","doi-asserted-by":"publisher","first-page":"7123","DOI":"10.1021\/bi901015d","article-title":"Properties of Arg481\nMutants of the Aa3-Type Cytochrome\nc Oxidase from Rhodobacter Sphaeroides Suggest That Neither R481 nor\nthe Nearby D-Propionate of Heme A3 Is Likely To Be the Proton Loading\nSite of the Proton Pump","volume":"48","author":"Lee","year":"2009","journal-title":"Biochemistry"},{"issue":"31","key":"2026102809104437600_cit40","doi-asserted-by":"publisher","first-page":"10457","DOI":"10.1021\/bi050283d","article-title":"An Arginine\nto Lysine Mutation in\nthe Vicinity of the Heme Propionates Affects the Redox Potentials\nof the Hemes and Associated Electron and Proton Transfer in Cytochrome\nc Oxidase","volume":"44","author":"Mills","year":"2005","journal-title":"Biochemistry"},{"issue":"33","key":"2026102809104437600_cit41","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2026169118","article-title":"Hydrogen Bonding\nRearrangement by\na Mitochondrial Disease Mutation in Cytochrome Bc1 Perturbs Heme bH\nRedox Potential and Spin State","volume":"118","author":"Kuleta","year":"2021","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"issue":"7","key":"2026102809104437600_cit42","doi-asserted-by":"publisher","first-page":"4371","DOI":"10.1074\/jbc.M509582200","article-title":"Structural and Mutagenesis Studies on the Cytochrome\nc Peroxidase from Rhodobacter Capsulatus Provide New Insights into\nStructure-Function Relationships of Bacterial Di-Heme Peroxidases*","volume":"281","author":"De Smet","year":"2006","journal-title":"J. Biol. 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Biol. Chem."},{"issue":"24","key":"2026102809104437600_cit47","doi-asserted-by":"publisher","first-page":"7585","DOI":"10.1021\/ja00492a025","article-title":"Iron Porphyrin Phenoxides:\nModels for Some Hemoglobin Mutants","volume":"100","author":"Ainscough","year":"1978","journal-title":"J. Am. 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Acta,\nProtein Struct."},{"issue":"17","key":"2026102809104437600_cit52","doi-asserted-by":"publisher","first-page":"5169","DOI":"10.1021\/ja00433a019","article-title":"Nature\nof the Iron-Ligand\nBond in Ferrous Low Spin Hemoproteins Studied by Resonance Raman Scattering","volume":"98","author":"Kitagawa","year":"1976","journal-title":"J. Am. Chem. Soc."},{"issue":"2","key":"2026102809104437600_cit53","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1021\/ja00809a004","article-title":"Resonance Raman\nSpectra of Heme Proteins. Effects of\nOxidation and Spin State","volume":"96","author":"Spiro","year":"1974","journal-title":"J. Am. Chem. 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