Evidence map›Paper›PMID 20023300›Full record

ArticleThe Journal of biological chemistry2010

Modifications of protein environment of the [2Fe-2S] cluster of the bc1 complex: effects on the biophysical properties of the rieske iron-sulfur protein and on the kinetics of the complex.

Sangmoon Lhee, Derrick R J Kolling, Satish K Nair, Sergei A Dikanov, Antony R Crofts

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. The cytochrome bPhotosynthesis research · 2024
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Sangmoon LheeCenter for Biophysics and Computational Biology, University of Illinois, Urbana, Illinois 61801, USA.
Derrick R J Kolling
Satish K Nair
Sergei A Dikanov
Antony R Crofts
University of Illinois Urbana-Champaign · USUrbana University · US

Funding

MOLECULAR ARCHITECTURE OF UQH2: CYTC2 OXIDOREDUCTASER01GM035438 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI CROFTS, ANTONY R. · 1986 to 2011
$3.3M
Structure of reaction intermediates in the bc1 complexR01GM062954 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI DIKANOV, SERGEI A · 2002 to 2010
$2.2M
PULSED X BAND EPR SPECTROMETER FOR BIOMEDICAL RESEARCHS10RR015878 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI BELFORD, R LINN · 2001 to 2001
$489k
NCRR NIH HHS S10-RR15878NIGMS NIH HHS GM35438NIGMS NIH HHS GM62954NIGMS NIH HHS R01 GM035438NIGMS NIH HHS R01 GM062954
6 · The paper itself

Abstract

The rate-determining step in the overall turnover of the bc(1) complex is electron transfer from ubiquinol to the Rieske iron-sulfur protein (ISP) at the Q(o)-site. Structures of the ISP from Rhodobacter sphaeroides show that serine 154 and tyrosine 156 form H-bonds to S-1 of the [2Fe-2S] cluster and to the sulfur atom of the cysteine liganding Fe-1 of the cluster, respectively. These are responsible in part for the high potential (E(m)(,7) approximately 300 mV) and low pK(a) (7.6) of the ISP, which determine the overall reaction rate of the bc(1) complex. We have made site-directed mutations at these residues, measured thermodynamic properties using protein film voltammetry to evaluate the E(m) and pK(a) values of ISPs, explored the local proton environment through two-dimensional electron spin echo envelope modulation, and characterized function in strains S154T, S154C, S154A, Y156F, and Y156W. Alterations in reaction rate were investigated under conditions in which concentration of one substrate (ubiquinol or ISP(ox)) was saturating and the other was varied, allowing calculation of kinetic terms and relative affinities. These studies confirm that H-bonds to the cluster or its ligands are important determinants of the electrochemical characteristics of the ISP, likely through electron affinity of the interacting atom and the geometry of the H-bonding neighborhood. The calculated parameters were used in a detailed Marcus-Brønsted analysis of the dependence of rate on driving force and pH. The proton-first-then-electron model proposed accounts naturally for the effects of mutation on the overall reaction.

Indexed as

Antimycin ABiophysicsCircular DichroismElectrochemistryElectron Spin Resonance SpectroscopyElectron TransportElectron Transport Complex IIIHydrogen BondingHydrogen-Ion ConcentrationIron-Sulfur ProteinsModels, ChemicalMutagenesis, Site-DirectedMutationRhodobacter sphaeroidesUbiquinoneAntimycin AElectron Transport Complex IIIIron-Sulfur ProteinsubiquinolUbiquinone

Identifiers

PMID20023300
PMCPMC2838342
OpenAlexW2132442880

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.