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Zoology and wildlife conservation

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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

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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)

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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

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Subjects list: Research, Hemoglobin synthesis
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