ReviewBiochimica et biophysica acta. Proteins and proteomics2018
Spectroscopic studies of the cytochrome P450 reaction mechanisms.
Review in Biochimica et biophysica acta. Proteins and proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 76 citations in OpenAlex.
- Natural astaxanthin enhances testosterone synthesis by improving mitochondrial function and reducing oxidative stress in Leydig cells.Poultry science · 2026Article
- Functional characterization of steroid hydroxylation by cytochrome P450 enzymes from Rhodococcus erythropolis KB1.Microbial cell factories · 2026Article
- Enhanced Catalytic Performance of P450 Monooxygenase CYP11B1 by Constructing Fusion Protein with Preferred Reductase Domain and Linker.Applied biochemistry and biotechnology · 2026Article
- From Transient to Metastable: Generation, Characterization, and Biomimetic Reactivity Studies of Well-Defined Heme Peroxynitrite Model Systems.Journal of the American Chemical Society · 2025Article
- Redox partner exchanges between spatially confined complexes control the coupling effect of cytochrome bScientific reports · 2025Article
- Stabilization of the Ferryl═Oxoheme Form ofJournal of the American Chemical Society · 2025Article
- Biotechnological production of terpenoids using cell factories.Frontiers in pharmacology · 2025Review
- Biosynthesis of eriodictyol in citrus waster by endowing P450BM3 activity of naringenin hydroxylation.Applied microbiology and biotechnology · 2024Article
- Article
- Melatonin Activation by Human Cytochrome P450 Enzymes: A Comparison between Different Isozymes.Molecules (Basel, Switzerland) · 2023Article
- Dual factors required for cytochrome-P450-mediated hydrocarbon ring contraction in bacterial gibberellin phytohormone biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Solvent isotope effects in the catalytic cycle of P450 CYP17A1: Computational modeling of the hydroxylation and lyase reactions.Journal of inorganic biochemistry · 2023Article
- The Development of Tungsten Biochemistry-A Personal Recollection.Molecules (Basel, Switzerland) · 2023Review
- Solution phase refinement of active site structure using 2D NMR and judiciouslyJournal of inorganic biochemistry · 2023Article
- Dynamic Ir(III) Photosensors for the Major Human Drug-Metabolizing Enzyme Cytochrome P450 3A4.Inorganic chemistry · 2023Article
- Melatonin Activation by Cytochrome P450 Isozymes: How Does CYP1A2 Compare to CYP1A1?International journal of molecular sciences · 2023Article
- Design of Cytochrome P450 1B1 InhibitorsJournal of medicinal chemistry · 2023Article
- Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 fromInternational journal of molecular sciences · 2022Article
- Modulating the Coupling Efficiency of P450 BM3 by Controlling Water Diffusion through Access Tunnel Engineering.ChemSusChem · 2022Article
- Transcriptome analysis of Harumi tangor fruits: Insights into interstock-mediated fruit quality.Frontiers in plant science · 2022Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The cytochrome P450 monooxygenases (P450s) are thiolate heme proteins that can, often under physiological conditions, catalyze many distinct oxidative transformations on a wide variety of molecules, including relatively simple alkanes or fatty acids, as well as more complex compounds such as steroids and exogenous pollutants. They perform such impressive chemistry utilizing a sophisticated catalytic cycle that involves a series of consecutive chemical transformations of heme prosthetic group. Each of these steps provides a unique spectral signature that reflects changes in oxidation or spin states, deformation of the porphyrin ring or alteration of dioxygen moieties. For a long time, the focus of cytochrome P450 research was to understand the underlying reaction mechanism of each enzymatic step, with the biggest challenge being identification and characterization of the powerful oxidizing intermediates. Spectroscopic methods, such as electronic absorption (UV-Vis), electron paramagnetic resonance (EPR), nuclear magnetic resonance (NMR), electron nuclear double resonance (ENDOR), Mössbauer, X-ray absorption (XAS), and resonance Raman (rR), have been useful tools in providing multifaceted and detailed mechanistic insights into the biophysics and biochemistry of these fascinating enzymes. The combination of spectroscopic techniques with novel approaches, such as cryoreduction and Nanodisc technology, allowed for generation, trapping and characterizing long sought transient intermediates, a task that has been difficult to achieve using other methods. Results obtained from the UV-Vis, rR and EPR spectroscopies are the main focus of this review, while the remaining spectroscopic techniques are briefly summarized. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.