Research graph
References from Structural and Functional Characterisation of a Metagenome‐Derived CYP108D18 Reveals an Unusual Dioxygen‐Bound State and Selective Hydrocarbon Hydroxylation. Local targets link to admitted publications; unresolved targets remain external evidence.
Accurate Structure Prediction of Biomolecular Interactions With AlphaFold 3
10.1038/s41586-024-07487-w · 2024 · External reference
PHENIX: A Comprehensive Python‐Based System for Macromolecular Structure Solution
10.1107/s0907444909052925 · 2010 · External reference
H++ 3.0: Automating pK Prediction and the Preparation of Biomolecular Structures for Atomistic Molecular Modeling and Simulations
10.1093/nar/gks375 · 2012 · External reference
A Cytochrome P450 Class I Electron Transfer System From Novosphingobium aromaticivorans
10.1007/s00253-009-2234-y · 2010 · External reference
P450 Enzymes From the Bacterium Novosphingobium aromaticivorans
10.1016/j.bbrc.2007.06.119 · 2007 · External reference
Crystal Structure of CYP199A2, a Para‐Substituted Benzoic Acid Oxidizing Cytochrome P450 From Rhodopseudomonas palustris
10.1016/j.jmb.2008.08.033 · 2008 · External reference
Structure and Function of CYP108D1 From Novosphingobium aromaticivorans DSM12444: An Aromatic Hydrocarbon‐Binding P450 Enzyme
10.1107/s090744491200145x · 2012 · External reference
Transition Metal Complexes as Mediator‐Titrants in Protein Redox Potentiometry
10.1007/s00775-006-0148-z · 2006 · External reference
Midpoint Redox Potentials of Plant and Algal Ferredoxins
10.1042/bj1680205 · 1977 · External reference
AmberTools
10.1021/acs.jcim.3c01153 · 2023 · External reference
Different Geometric Requirements for Cytochrome P450‐Catalyzed Aliphatic Versus Aromatic Hydroxylation Results in Chemoselective Oxidation
10.1021/acscatal.1c05483 · 2022 · External reference
Redox Control of the Catalytic Cycle of Flavocytochrome P‐450 BM3
10.1021/bi971085s · 1997 · External reference
Coot: Model‐Building Tools for Molecular Graphics
10.1107/s0907444904019158 · 2004 · External reference
Isolation and Characterization of a Subsurface Bacterium Capable of Growth on Toluene, Naphthalene, and Other Aromatic Compounds
10.1128/aem.57.3.796-803.1991 · 1991 · External reference
Unresolved reference
External reference
Cooperative Substrate Binding Controls Catalysis in Bacterial Cytochrome P450terp (CYP108A1)
10.1021/jacs.2c12388 · 2023 · External reference
Catalytic Mechanism of Cytochrome P‐450: Evidence for a Distal Charge Relay
10.1021/ja00048a081 · 1992 · External reference
Cymredoxin, a [2Fe–2S] Ferredoxin, Supports Catalytic Activity of the p‐Cymene Oxidising P450 Enzyme CYP108N12
10.1016/j.abb.2023.109549 · 2023 · External reference
CYP108N12 Initiates p‐Cymene Biodegradation in Rhodococcus globerulus
10.1016/j.abb.2022.109410 · 2022 · External reference
Unrivalled Diversity: The Many Roles and Reactions of Bacterial Cytochromes P450 in Secondary Metabolism
10.1039/c7np00063d · 2018 · External reference
Measurement of Cytochrome P450 and NADPH–Cytochrome P450 Reductase
10.1038/nprot.2009.121 · 2009 · External reference
Cytochrome P‐450 Substrate and Effector Interactions
10.1111/j.1749-6632.1973.tb47590.x · 1973 · External reference
Crystal Structure and Refinement of Cytochrome P450terp at 2.3 Å Resolution
10.1016/0022-2836(94)90019-1 · 1994 · External reference
Cytochrome P450cin (CYP176A), Isolation, Expression, and Characterization
10.1074/jbc.m203382200 · 2002 · External reference
Cloning, Expression and Purification of Cindoxin, an Unusual FMN‐Containing Cytochrome P450 Redox Partner
10.1002/cbic.201000119 · 2010 · External reference
The Impact of Metagenomics on Biocatalysis
10.1002/ange.202402316 · 2024 · External reference
Analysis of the Domain Properties of the Novel Cytochrome P450 RhF
10.1016/j.febslet.2005.03.016 · 2005 · External reference
Uncoupling of the Cytochrome P‐450cam Monooxygenase Reaction by a Single Mutation, Threonine‐252 to Alanine or Valine: Possible Role of the Hydroxy Amino Acid in Oxygen Activation
10.1073/pnas.86.20.7823 · 1989 · External reference
Flavodoxin and NADPH‐Flavodoxin Reductase From Escherichia coli Support Bovine Cytochrome P450c17 Hydroxylase Activities
10.1016/s0021-9258(18)46999-2 · 1994 · External reference
XDS
10.1107/s0907444909047337 · 2010 · External reference
Characterisation of the Thermophilic P450 CYP116B305 Identified Using Metagenomics‐Derived Sequence Data From an Australian Hot Spring
10.1007/s00253-025-13521-2 · 2025 · External reference
Characterization of a Cytochrome P450 Monooxygenase Capable of High Molecular Weight PAHs Oxidization From Rhodococcus sp. P14
10.1016/j.procbio.2016.07.024 · 2016 · External reference
Crystal Structures of Substrate‐Free and Nitrosyl Cytochrome P450cin: Implications for O2 Activation
10.1021/bi300666u · 2012 · External reference
Unresolved reference
2016 · External reference
ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters From ff99SB
10.1021/acs.jctc.5b00255 · 2015 · External reference
Phaser Crystallographic Software
10.1107/s0021889807021206 · 2007 · External reference
Characterization of a Cytochrome P450 From the Acidothermophilic Archaea Sulfolobus solfataricus
10.1006/bbrc.1998.9584 · 1998 · External reference
Blu‐Ice and the Distributed Control System: Software for Data Acquisition and Instrument Control at Macromolecular Crystallography Beamlines
10.1107/s0909049502015170 · 2002 · External reference
Using Molecular Dynamics to Probe the Structural Basis for Enhanced Stability in Thermal Stable Cytochromes P450
10.1021/bi100929x · 2010 · External reference
UCSF ChimeraX: Tools for Structure Building and Analysis
10.1002/pro.4792 · 2023 · External reference
Kinetics of the Reversible Inhibition of Enzyme‐Catalysed Reactions by Tight‐Binding Inhibitors
10.1016/0005-2744(69)90420-3 · 1969 · External reference
Crystal Structures of the Ferrous Dioxygen Complex of Wild‐Type Cytochrome P450eryF and Its Mutants, A245S and A245T
10.1074/jbc.m501732200 · 2005 · External reference
Crystallographic Study on the Dioxygen Complex of Wild‐Type and Mutant Cytochrome P450cam
10.1074/jbc.m505261200 · 2005 · External reference
The Cytochrome P450 Homepage
10.1186/1479-7364-4-1-59 · 2009 · External reference
Putidaredoxin Reductase and Putidaredoxin. Cloning, Sequence Determination, and Heterologous Expression of the Proteins
10.1016/s0021-9258(19)39292-0 · 1990 · External reference
Cytochrome P‐450terp. Isolation and Purification of the Protein and Cloning and Sequencing of Its Operon
10.1016/s0021-9258(19)49697-x · 1992 · External reference
X‐Ray–Induced Photoreduction of Heme Metal Centers Rapidly Induces Active‐Site Perturbations in a Protein‐Independent Manner
10.1074/jbc.ra120.014087 · 2020 · External reference
Conformational Plasticity and Structure/Function Relationships in Cytochromes P450
10.1089/ars.2010.3109 · 2010 · External reference
The 2.6‐A Crystal Structure of Pseudomonas putida Cytochrome P‐450
10.1016/s0021-9258(17)36209-9 · 1985 · External reference
Crystal Structure of Substrate‐Free Pseudomonas putida Cytochrome P‐450
10.1021/bi00366a049 · 1986 · External reference
High‐Resolution Crystal Structure of Cytochrome P450cam
10.1016/0022-2836(87)90190-2 · 1987 · External reference
Routine Microsecond Molecular Dynamics Simulations With AMBER on GPUs. 2. Explicit Solvent Particle Mesh Ewald
10.1021/ct400314y · 2013 · External reference
Mining and Unearthing Hidden Biosynthetic Potential
10.1038/s41467-021-24133-5 · 2021 · External reference
The Catalytic Pathway of Cytochrome P450cam at Atomic Resolution
10.1126/science.287.5458.1615 · 2000 · External reference
Quantum Mechanically Derived AMBER‐Compatible Heme Parameters for Various States of the Cytochrome P450 Catalytic Cycle
10.1002/jcc.21922 · 2012 · External reference
Fast, Scalable Generation of High‐Quality Protein Multiple Sequence Alignments Using Clustal Omega
10.1038/msb.2011.75 · 2011 · External reference
A Thermodynamic Model of Regulation: Modulation of Redox Equilibria in Camphor Monoxygenase
10.1073/pnas.73.4.1078 · 1976 · External reference
Haem Exposure as the Determinate of Oxidation–Reduction Potential of Haem Proteins
10.1038/275073a0 · 1978 · External reference
Oxidation‐Reduction Potentials and Stoichiometry of Electron Transfer in Ferredoxins
10.1016/0005-2728(68)90188-6 · 1968 · External reference
MEGA11: Molecular Evolutionary Genetics Analysis Version 11
10.1093/molbev/msab120 · 2021 · External reference
UniProt: The Universal Protein Knowledgebase in 2025
10.1093/nar/gkae1010 · 2025 · External reference
AutoDock Vina: Improving the Speed and Accuracy of Docking With a New Scoring Function, Efficient Optimization, and Multithreading
10.1002/jcc.21334 · 2010 · External reference
Protein Components of a Cytochrome P‐450 Linalool 8‐Methyl Hydroxylase
10.1016/s0021-9258(19)40020-3 · 1990 · External reference
CYP101J2, CYP101J3, and CYP101J4, 1,8‐Cineole‐Hydroxylating Cytochrome P450 Monooxygenases From Sphingobium yanoikuyae Strain B2
10.1128/aem.02067-16 · 2016 · External reference
Understanding the Role of the Essential Asp251 in Cytochrome P450cam Using Site‐Directed Mutagenesis, Crystallography, and Kinetic Solvent Isotope Effect
10.1021/bi980189f · 1998 · External reference
The Dynamics of Camphor in the Cytochrome P450 CYP101D2
10.1002/pro.2309 · 2013 · External reference
Combining Quantum Mechanics Methods With Molecular Mechanics Methods in ONIOM
10.1021/ct050289g · 2006 · External reference
10.1016/j.jmgm.2005.12.005
10.1016/j.jmgm.2005.12.005 · External reference
Cloning of a Potential Cytochrome P450 From the Archaeon Sulfolobus solfataricus
10.1016/0014-5793(96)00322-5 · 1996 · External reference
Molecular Characterization of a Class I P450 Electron Transfer System From Novosphingobium aromaticivorans DSM12444
10.1074/jbc.m110.118349 · 2010 · External reference
The Structure of CYP101D2 Unveils a Potential Path for Substrate Entry Into the Active Site
10.1042/bj20101017 · 2011 · External reference
Crystal Structure of a Thermophilic Cytochrome P450 From the Archaeon Sulfolobus solfataricus
10.1074/jbc.m004281200 · 2000 · External reference
Role of Active Site Water Molecules and Substrate Hydroxyl Groups in Oxygen Activation by Cytochrome P450 158A2
10.1074/jbc.m509220200 · 2005 · External reference
