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A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold

1 of 62 checkable references need attention · checked 2026-07-23

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References needing attention

does not resolve to a known work10.1042/0264-6021:3480321

The 61 checked references that resolve

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Selective oxygen transfer catalysed by heme peroxidases: synthetic and mechanistic aspects

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Significantly shorter Fe–S bond in cytochrome P450-I is consistent with greater reactivity relative to chloroperoxidase

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The role of the proximal ligand in heme enzymes

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Thirty years of heme peroxidase structural biology

resolves10.1039/b210426c

Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?

resolves10.1126/science.1193478

Cytochrome P450 Compound I: Capture, Characterization, and C-H Bond Activation Kinetics

resolves10.1073/pnas.1503340112

Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive

resolves10.1073/pnas.95.22.12825

In vitro evolution of horse heart myoglobin to increase peroxidase activity

resolves10.1038/nsb913

Crystal structure of the ascorbate peroxidase–ascorbate complex

resolves10.1016/S0969-2126(96)00035-4

The crystal structure of peanut peroxidase

resolves10.1016/S0006-3495(99)77056-6

Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution

resolves10.1038/nmeth.3179

Directed evolution of APEX2 for electron microscopy and proximity labeling

resolves10.1021/jacs.6b07029

A Chemically Programmed Proximal Ligand Enhances the Catalytic Properties of a Heme Enzyme

resolves10.1021/cb500032c

Genetic Incorporation of Histidine Derivatives Using an Engineered Pyrrolysyl-tRNA Synthetase

resolves10.1016/j.jmb.2009.10.030

An Enhanced System for Unnatural Amino Acid Mutagenesis in E. coli

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Studies on Modified Hemoglobins

resolves10.1021/jo00283a015

Methylimidazole-catalyzed ester hydrolysis: nonlinear kinetics

resolves10.1021/ja5054863

Systematic Tuning of Heme Redox Potentials and Its Effects on O2 Reduction Rates in a Designed Oxidase in Myoglobin

resolves10.1016/j.bbabio.2015.08.006

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

resolves10.1021/bi0261591

Substrate Binding and Catalytic Mechanism in Ascorbate Peroxidase: Evidence for Two Ascorbate Binding Sites

resolves10.1021/ja9914846

Formation and Catalytic Roles of Compound I in the Hydrogen Peroxide-Dependent Oxidations by His64 Myoglobin Mutants

resolves10.1021/ja970453c

Conversion of Myoglobin into a Peroxygenase: A Catalytic Intermediate of Sulfoxidation and Epoxidation by the F43H/H64L Mutant

resolves10.1016/S0021-9258(18)96096-5

Studies on Cytochrome c Peroxidase

resolves10.1006/abio.1997.2391

A Stable Nonfluorescent Derivative of Resorufin for the Fluorometric Determination of Trace Hydrogen Peroxide: Applications in Detecting the Activity of Phagocyte NADPH Oxidase and Other Oxidases

resolves10.1016/S0021-9258(18)81654-4

Reactions of the Protein Radical in Peroxide-treated Myoglobin

resolves10.1021/bi025835w

Role of Tyrosine-103 in Myoglobin Peroxidase Activity: Kinetic and Steady-State Studies on the Reaction of Wild-Type and Variant Recombinant Human Myoglobins with H2O2

resolves10.1042/bj2370613

Characterization of haem disorder by circular dichroism

resolves10.1016/S0022-2836(83)80080-1

Heme orientational disorder in reconstituted and native sperm whale myoglobin

resolves10.1007/s00775-016-1430-3

A new look at the role of thiolate ligation in cytochrome P450

resolves10.1126/science.1096897

Oxoiron(IV) in Chloroperoxidase Compound II Is Basic: Implications for P450 Chemistry

resolves10.1126/science.1244373

Iron(IV)hydroxide p K a and the Role of Thiolate Ligation in C–H Bond Activation by Cytochrome P450

resolves10.1016/S0021-9258(19)83923-6

Coordination structures and reactivities of compound II in iron and manganese horseradish peroxidases. A resonance Raman study.

resolves10.1016/S0021-9258(17)39637-0

Heme-linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe(IV)=O stretching vibration.

resolves10.1016/0167-4838(85)90301-2

Observation of the FeIVO stretching vibration of ferryl myoglobin by resonance Raman spectroscopy

resolves10.1021/ja503588n

Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pKa: Insight into Axial Ligand Tuning in Heme Protein Catalysis

resolves10.1021/ja054074s

Application of Badger's Rule to Heme and Non-Heme Iron−Oxygen Bonds: An Examination of Ferryl Protonation States

resolves10.1073/pnas.0810503106

Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine

resolves10.1002/anie.200901485

Calculated and Experimental Spin State of Seleno Cytochrome P450

resolves10.1038/nchem.2781

Characterization of a selenocysteine-ligated P450 compound I reveals direct link between electron donation and reactivity

resolves10.1021/ja211499q

Proximal Ligand Electron Donation and Reactivity of the Cytochrome P450 Ferric–Peroxo Anion

resolves10.1021/acs.biochem.5b00939

Kinetic Consequences of Introducing a Proximal Selenocysteine Ligand into Cytochrome P450cam

resolves10.1021/bi00052a031

Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase

resolves10.1007/s11426-014-5063-5

Functional tuning and expanding of myoglobin by rational protein design

resolves10.1073/pnas.1000526107

Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin

resolves10.1021/ja0015343

From Myoglobin to Heme-Copper Oxidase: Design and Engineering of a CuB Center into Sperm Whale Myoglobin

resolves10.1007/978-3-642-12627-7_4

Redox Potential of Peroxidases

resolves10.1073/pnas.1521664113

Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer

resolves10.1038/417463a

The catalytic pathway of horseradish peroxidase at high resolution

resolves10.1016/S0021-9258(18)90651-4

Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution.

resolves10.1074/jbc.274.5.2838

Effects of the Location of Distal Histidine in the Reaction of Myoglobin with Hydrogen Peroxide

resolves10.1016/S0010-8545(00)00234-4

Rational molecular design of a catalytic site: engineering of catalytic functions to the myoglobin active site framework

resolves10.1021/bi00233a009

Contributions of residue 45(CD3) and heme-6-propionate to the bimolecular and geminate recombination reactions of myoglobin

resolves10.1016/j.febslet.2013.12.030

A simple method for the determination of reduction potentials in heme proteins

resolves10.1111/j.1432-1033.1975.tb04000.x

Fractionation of Horseradish Peroxidase by Preparative Isoelectric Focusing, Gel Chromatography and Ion‐Exchange Chromatography

resolves10.1126/science.1218231

Linking Crystallographic Model and Data Quality

resolves10.1107/S090744499801405X

Efficient anisotropic refinement of macromolecular structures using FFT

resolves10.1107/S0907444904019158

Coot: model-building tools for molecular graphics

The 1 reference without a DOI — listed, not checked

no DOI — not checkedHemoglobin and Myoglobin in Their Reactions With Ligands

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