Evidence map›Paper›PMID 19345605›Full record

ArticleCurrent opinion in chemical biology2009

C-H bond activation in heme proteins: the role of thiolate ligation in cytochrome P450.

Michael T Green

Abstract read
PubMed Publisher
In one paragraph

Article in Current opinion in chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.2field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

73 citing papers in PubMed, 182 citations in OpenAlex.

  1. Article
  2. Article
  3. Oxidizable amino acids around cytochrome P450 hemes.Journal of inorganic biochemistry · 2026
    Article
  4. Article
  5. Article
  6. Intramolecular Oxo Atom Migration to theJournal of the American Chemical Society · 2025
    Article
  7. Insights into Active Site Cysteine Residues inInternational journal of molecular sciences · 2025
    Review
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  20. Review

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Michael T GreenDepartment of Chemistry, Penn State University, University Park, 16802, United States. mtg10@psu.edu
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of cytochrome P450 to functionalize unactivated hydrocarbons at physiological temperature and pressure has attracted considerable interest from the chemical community. One of the more intriguing aspects of cytochrome P450 is the enzyme's use of a thiolate-ligated heme to perform demanding two-electron oxidations. This coordination is unusual, given that thiolate ligation can significantly decrease a heme reduction potential. In an effort to understand Nature's use of a donating thiolate in cytochrome P450, we have undertaken a systematic study of the high-valent forms of thiolate ligated heme proteins. Our investigations have revealed that the ferryl forms of these enzymes are basic. The basic ferryls afforded by thiolate ligation bias cytochrome P450 toward H-atom abstraction, creating an oxidant that cleaves CH bonds while avoiding unwanted oxidations of the protein superstructure. Recent synthetic work supports this hypothesis.

Indexed as

Cytochrome P-450 Enzyme SystemEnzyme ActivationHemeproteinsOxidation-ReductionCytochrome P-450 Enzyme SystemHemeproteins

Identifiers

PMID19345605
OpenAlexW2059692975

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.