Evidence map›Paper›PMID 17602662›Full record

ArticleBiochemistry2007

Axial ligation and stoichiometry of heme centers in adrenal cytochrome b561.

Yury Kamensky, Wen Liu, Ah-Lim Tsai, Richard J Kulmacz, Graham Palmer

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Cecytb-2, a CytochromeBiomolecules · 2025
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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.

Yury KamenskyDepartment of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251, USA. yuryk@bioc.rice.edu
Wen Liu
Ah-Lim Tsai
Richard J Kulmacz
Graham Palmer
The University of Texas Health Science Center at Houston · USRice University · US

Funding

STRUCTURE/FUNCTION &REACTION MECHANISM OF PGHS &ENOSR01GM044911 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI TSAI, AH-LIM · 1992 to 2008
$2.2M
Structure and function of cytochrome b561R01GM080575 · NIGMS · RICE UNIVERSITY · PI PALMER, GRAHAM A. · 2007 to 2010
$1.1M
NIGMS NIH HHS GM44911NIGMS NIH HHS R01 GM044911NIGMS NIH HHS R01 GM080575
6 · The paper itself

Abstract

Cytochrome (cyt) b561 transports electrons across the membrane of chromaffin granules (CG) present in the adrenal medulla, supporting the biosynthesis of norepinephrine in the CG matrix. We have conducted a detailed characterization of cyt b561 using electron paramagnetic resonance (EPR) and optical spectroscopy on the wild-type and mutant forms of the cytochrome expressed in insect cells. The gz = 3.7 (low-potential heme) and gz = 3.1 (high-potential heme) signals were found to represent the only two authentic hemes of cyt b561; models that propose smaller or greater amounts of heme can be ruled out. We identified the axial ligands to hemes in cyt b561 by mutating four conserved histidines (His54 and His122 at the matrix-side heme center and His88 and His161 at the cytoplasmic-side heme center), thus confirming earlier structural models. Single mutations of any of these histidines produced a constellation of spectroscopic changes that involve not one but both heme centers. We hypothesize that the two hemes and their axial ligands in cyt b561 are integral parts of a structural unit that we term the "kernel". Histidine to glutamine substitutions in the cytoplasmic-side heme center but not in the matrix-side heme center led to the retention of a small fraction of the low-potential heme with gz = 3.7. We provisionally assign the low-potential heme to the matrix side of the membrane; this arrangement suggests that the membrane potential modulates electron transport across the CG membrane.

Indexed as

Adrenal MedullaAnimalsCattleCell MembraneCytochrome b GroupCytoplasmElectron Spin Resonance SpectroscopyHemeHistidineLigandsModels, BiologicalMutationRecombinant Proteinscytochrome b561Cytochrome b GroupHemeHistidineLigandsRecombinant Proteins

Identifiers

PMID17602662
PMCPMC2551744
OpenAlexW2089670569

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.