Heme Iron Nitrosyl Complex of MauG Reveals an Efficient Redox Equilibrium between Hemes with Only One Heme Exclusively Binding Exogenous Ligands

Rong Fu Fange Liu Victor L. Davidson and Aimin Liu

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Heme Iron Nitrosyl Complex of MauG Reveals an Efficient Redox Equilibrium between Hemes with Only One Heme Exclusively Binding Exogenous Ligands

机译：MauG的血红素铁亚硝酰基配合物揭示了血红素之间的高效氧化还原平衡，只有一个血红素能独家结合外源配体。

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MauG is a diheme enzyme that oxidizes twonprotein-bound tryptophan residues to generate a catalyticntryptophan tryptophylquinone cofactor within methyl-namine dehydrogenase. Upon the two-electron oxidationnof bis-ferric MauG, the two c-type hemes exist as a spin-nuncoupled bis-Fe(IV) species with only one binding oxy-ngen, which is chemically equivalent to a single ferrylnheme plus a π porphyrin cation radical (Li, X. et al.n(2008) Proc. Natl. Acad. Sci. U.S.A. 105, 8597-8600).nThe EPR spectrum of the nitrosyl complex of fully reducednMauG shows a single six-coordinate Fe(II)-NO species,nwhich is characteristic of a histidine-ligated Fe(II)-NOnmoiety in the heme environment. Exposure of partiallynreduced MauG to NO reveals a redox equilibrium withnfacile electron transfer between hemes but with only onenbinding nitric oxide. Thus, the second heme is able tonstabilize all three redox states of iron (Fe(II), Fe(III), andnFe(IV)) in a six-coordinate protein-bound heme withoutnbinding exogenous ligands. This is unprecedented behaviornfor a protein-bound heme for which each of these redoxnstates is relevant to the overall catalytic mechanism. Thenresults also illustrate the electronic communication bet-nween the two iron centers, which function as a diheme unitnrather than independent heme cofactors.

机译：MauG是一种双血红素酶，可氧化结合二蛋白的色氨酸残基，从而在甲基-胺脱氢酶中产生催化性色氨酸色氨酸醌辅因子。双铁MauG的双电子氧化后，两个c型血红素以自旋-非偶合双Fe（IV）形式存在，仅具有一个结合氧，化学上等效于单个亚铁血红素加上π卟啉阳离子自由基（Li，X. et al.n（2008）Proc.Natl.Acad.Sci.USA 105，8597-8600）.n完全还原的nMauG的亚硝酰基配合物的EPR谱显示单个六配位的Fe（II） -在血红素环境中组氨酸连接的Fe（II）-NO的特征。部分还原的MauG暴露于NO揭示了氧化还原平衡，其中血红素之间的电子转移不容易，但仅具有一氧化氮。因此，第二血红素能够在不与外源配体结合的六坐标蛋白质结合的血红素中使铁的所有三个氧化还原态（Fe（II），Fe（III）和nFe（IV））稳定。对于蛋白质结合的血红素而言，这是前所未有的行为，对于这些蛋白质而言，这些氧化还原态均与整体催化机制有关。然后结果还说明了两个铁心之间的电子通信，它们起着双血红素的作用，而不是独立的血红素的辅因子。

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《Biochemistry》 |2009年第49期|p.11603-11605|共3页
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Rong Fu Fange Liu Victor L. Davidson and Aimin Liu;
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‡Department of Chemistry, Georgia State University, P.O. Box 4098, Atlanta, Georgia 30302, and §Department of Biochemistry, TheUniversity ofMississippiMedical Center, Jackson,Mississippi 39216.) Current address: Department of Neurology, Emory University,Atlanta, GA 30322.;

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2. Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy. [J] . Rappaport F, Vos MH, Borisov VB Biochimica et biophysica acta. Bioenergetics . 2010,第9期

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3. Modeling the cis-Oxo-Labile binding site motif of non-heme iron oxygenases: Water exchange and oxidation reactivity of a non-heme iron(IV)-Oxo compound bearing a tripodal tetradentate ligand [J] . Company A., Prat I., Frisch J.R., Chemistry: A European journal . 2011,第5期

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4. Heme Binding Analysis of Heme Regulatory Motifs of Rat Heme Oxygenase-2 [C] . Tomomi Ueda, Shinya Koga, Yuichiro Higashimoto Japanese peptide symposium . 2010

机译：大鼠血红素氧氨基氨基酶-2血红素调节基序血红素结合分析
5. Part I: Spectroscopic investigations of the heme active site coordination structure of the exogenous ligand-free myoglobin cavity mutant H93G and investigations of H93G-thiolate adducts as structural and mechanistic model systems for cytochrome P450. Part II: Spectroscopic investigations of proximal heme iron ligation in two novel halogenating and dehalogenating peroxidase enzymes isolated from marine sources. [D] . Roach, Mark Patrick. 1997

机译：第一部分：无外源配体的肌红蛋白腔突变体H93G的血红素活性位点配位结构的光谱研究，以及作为细胞色素P450结构和机理模型系统的H93G-硫醇盐加合物的研究。第二部分：从海洋来源分离的两种新型卤化和脱卤过氧化物酶中近端血红素铁连接的光谱研究。
6. Heme Iron Nitrosyl Complex of MauG Reveals an Efficient Redox Equilibrium Between Hemes with Only One Heme Exclusively Binding Exogenous Ligands [O] . Rong Fu, Fange Liu, Victor L. Davidson, -1

机译：血红素铁亚硝基复杂mauG的揭示一个高效的氧化还原平衡血红素之间仅一个与血红素结合独占外源性配体
7. Heme Iron Nitrosyl Complex of MauG Reveals an Efficient Redox Equilibrium between Hemes with Only One Heme Exclusively Binding Exogenous Ligands [O] . Rong Fu, Fange Liu, Victor L. Davidson, 2009

机译：血红素铁亚硝基络合物揭示了血糖之间有效的氧化还原平衡，只有一个血红素，专门有一个血红素，专门结合外源性配体

Heme Iron Nitrosyl Complex of MauG Reveals an Efficient Redox Equilibrium between Hemes with Only One Heme Exclusively Binding Exogenous Ligands

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