Abstracts - faqs.org

Abstracts

Zoology and wildlife conservation

Search abstracts:
Abstracts » Zoology and wildlife conservation

Ascaris haemoglobin is a nitric oxide-activated 'deoxygenase.'

Article Abstract:

It has been possible to identify new nitric oxide (NO) chemistry involving enzymatic activity of a haem-thiol-NO redox triad. It was established that haemoglobin of the parasitic nematode Ascaris lumbricoides enzymatically consumes oxygen in a reaction driven by NO, thus keeping the perienteric fluid hypoxic. It is suggested that Ascaris haemoglobin acts as a 'deoxygenase,' with NO being used to detoxify oxygen.

Author: Stamler, Jonathan S., Bonaventura, Joseph, Gow, Andrew J., Minning, Dena M., Braun, Rod, Dewhirst, Mark, Goldberg, Daniel E.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
Physiological aspects, Ascaris

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA

Structure of the apoptotic protease-activating factor 1 bound to ADP

Article Abstract:

A study is carried out on the apoptotic protease-activating factor-1 (Apaf-1) that controls caspase activation downstream of mitochondria. The study reports about the 2,2-A crystal structure of an ADP-bound, WD40-deleted apoptotic protease-activating factor-1 (Apaf-1), which reveals the molecular mechanism by which Apaf-1exists in an inactive state before ATP bindings.

Author: Yigong Shi, Schwarzenbacher, Robert, Riedi, Stefan J., Wenyu Li, Yang Chao
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
Drugs, Adenosine triphosphate, ATP, Structure-activity relationships (Pharmacology), Adenosine diphosphate, Structure-activity relationship (Pharmacology)

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA

Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem

Article Abstract:

The crystal structure of the ferric alpha-haemoglobin--alpha haemoglobin stabilizing protein (AHSP) complex at 2.4-angstrom resolution is reported. Findings reveal a striking bis-histidyl configuration in which both the proximal and the distal histidines coordinate the haem iron atom.

Author: Yigong Shi, Liang Feng, Suiping Zhou, Gell, David A., Lichuan Gu, Gow, Andrew J., Weiss, Mitchell J., Mackay, Joel P.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
United States, Crystals, Crystal structure, Oxidation-reduction reaction, Oxidation-reduction reactions

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Hemoglobin synthesis
Similar abstracts:
  • Abstracts: Freaks of nature? Joint suits aim to weed out agencies' red tape. Geneticists play the numbers game in vain
  • Abstracts: Structure of influenza virus haemagglutinin complexed with a neutralizing antibody. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
  • Abstracts: Optimal isotope labeling for NMR protein structure determinations. Lead isotopes reveal bilateral asymmetry and vertical continuity in the Hawaiian mantle plume
  • Abstracts: New Madrid in motion. Space geodetic evidence for rapid strain rates in the New Madrid seismic zone of central USA
  • Abstracts: France eyes role in US mission to retrieve rocks from Mars. Opinion divided on images of Martian 'ocean'. Going underground
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2018 Advameg, Inc.