The circularly permuted globin domain of androglobin exhibits atypical heme stabilization and nitric oxide interaction

Author:

Reeder Brandon J.1ORCID,Deganutti Giuseppe12ORCID,Ukeri John1,Atanasio Silvia1,Svistunenko Dimitri A.1ORCID,Ronchetti Christopher1,Mobarec Juan Carlos12ORCID,Welbourn Elizabeth1ORCID,Asaju Jeffrey1,Vos Marten H.3ORCID,Wilson Michael T.1,Reynolds Christopher A.12

Affiliation:

1. School of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK

2. Centre for Health and Life Sciences (CHLS), Alison Gingell Building, Coventry, CV1 5FB, UK

3. LOB, CNRS, INSERM, École Polytechnique, Institut Polytechnique de Paris, 91128 Palaiseau, France

Abstract

Since the discovery of androglobin, a multi-domain hemoglobin associated with ciliogenesis and spermatogenesis, there has been little advance in the knowledge of the biochemical and structural properties of this member of the hemoglobin superfamily.

Funder

Biotechnology and Biological Sciences Research Council

Publisher

Royal Society of Chemistry (RSC)

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