ArticleBiochemistry2010
Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine .
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 48 citations in OpenAlex.
- Antioxidant Nanozymes: Mechanisms, Activity Manipulation, and Applications.Micromachines · 2023Review
- Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.Biochemistry · 2023Article
- A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.Journal of the American Chemical Society · 2020Article
- A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.Nature communications · 2019Article
- Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Biochemistry · 2018Review
- Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.FEBS letters · 2017Article
- Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer.The Biochemical journal · 2016Article
- Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.Biochimica et biophysica acta · 2015Article
- Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.Angewandte Chemie (International ed. in English) · 2015Article
- Bis-Fe(IV): nature's sniper for long-range oxidation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.Chemical reviews · 2014Review
- Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.Biochemistry · 2014Article
- MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Archives of biochemistry and biophysics · 2014Review
- Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.Biochemistry · 2013Article
- Structure of the processive rubber oxygenase RoxA from Xanthomonas sp.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis.FEBS letters · 2013Article
- Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.Dalton transactions (Cambridge, England : 2003) · 2013Review
- Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.Annual review of biochemistry · 2013Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The diheme enzyme MauG catalyzes the posttranslational modification of a precursor protein of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. It catalyzes three sequential two-electron oxidation reactions which proceed through a high-valent bis-Fe(IV) redox state. Tyr294, the unusual distal axial ligand of one c-type heme, was mutated to His, and the crystal structure of Y294H MauG in complex with preMADH reveals that this heme now has His-His axial ligation. Y294H MauG is able to interact with preMADH and participate in interprotein electron transfer, but it is unable to catalyze the TTQ biosynthesis reactions that require the bis-Fe(IV) state. This mutation affects not only the redox properties of the six-coordinate heme but also the redox and CO-binding properties of the five-coordinate heme, despite the 21 Å separation of the heme iron centers. This highlights the communication between the hemes which in wild-type MauG behave as a single diheme unit. Spectroscopic data suggest that Y294H MauG can stabilize a high-valent redox state equivalent to Fe(V), but it appears to be an Fe(IV)═O/π radical at the five-coordinate heme rather than the bis-Fe(IV) state. This compound I-like intermediate does not catalyze TTQ biosynthesis, demonstrating that the bis-Fe(IV) state, which is stabilized by Tyr294, is specifically required for this reaction. The TTQ biosynthetic reactions catalyzed by wild-type MauG do not occur via direct contact with the Fe(IV)═O heme but via long-range electron transfer through the six-coordinate heme. Thus, a critical feature of the bis-Fe(IV) species may be that it shortens the electron transfer distance from preMADH to a high-valent heme iron.
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