Literature DB >> 14560666

Microbial globins.

Guanghui Wu1, Laura M Wainwright, Robert K Poole.   

Abstract

Globins are an ancient and diverse superfamily of proteins. The globins of microorganisms were relatively ignored for many decades after their discovery by Warburg in the 1930s and rediscovery by Keilin in the 1950s. The relatively recent focus on them has been fuelled by recognition of their structural diversity and fine-tuning to fulfill (probably) discrete functions but particularly by the finding that a major role of certain globins is in protection from the stresses caused by exposure to nitric oxide (NO)--itself a molecule that has attracted intense curiosity recently. At least three classes of microbial globin are recognised, all having features of the classical globin protein fold. The first class is typified by the myoglobin-like haemprotein Vgb from the bacterium Vitreoscilla, which has attracted considerable attention because of its ability to improve growth and metabolism for biotechnological gain in a variety of host cells, even though its physiological function is not fully understood. The truncated globins are widely distributed in bacteria, microbial eukaryotes as well as plants and are characterised by being 20-40 residues shorter than Vgb. The polypeptide is folded into a two-over-two helical structure while retaining the essential features of the globin superfamily. Roles in oxygen and NO metabolism have been proposed. The third and best understood class comprises the flavohaemoglobins, which were first discovered and partly characterised in yeast. These are distinguished by the presence of an additional domain with binding sites for FAD and NAD(P)H. Widely distributed in bacteria, these proteins undoubtedly confer protection from NO and nitrosative stresses, probably by direct consumption of NO. However, a bewildering array of enzymatic capabilities and the presence of an active site in the haem pocket reminiscent of peroxidases hint at other functions. A full understanding of microbial globins promises advances in controlling the interactions of pathogenic bacteria with their animal and plant hosts, and manipulations of microbial oxygen transfer with biotechnological applications.

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Year:  2003        PMID: 14560666     DOI: 10.1016/s0065-2911(03)47005-7

Source DB:  PubMed          Journal:  Adv Microb Physiol        ISSN: 0065-2911            Impact factor:   3.517


  23 in total

1.  What are the origins and phylogeny of plant hemoglobins?

Authors:  Serge N Vinogradov; David Hoogewijs; Raúl Arredondo-Peter
Journal:  Commun Integr Biol       Date:  2011-07-01

2.  Evolution of structural shape in bacterial globin-related proteins.

Authors:  Lorraine Marsh
Journal:  J Mol Evol       Date:  2006-04-11       Impact factor: 2.395

3.  Novel flavohemoglobins of mycobacteria.

Authors:  Sanjay Gupta; Sudesh Pawaria; Changyuan Lu; Syun-Ru Yeh; Kanak L Dikshit
Journal:  IUBMB Life       Date:  2011-04-13       Impact factor: 3.885

4.  A phylogenetic and structural analysis of truncated hemoglobins.

Authors:  David A Vuletich; Juliette T J Lecomte
Journal:  J Mol Evol       Date:  2006-02-10       Impact factor: 2.395

5.  Three globin lineages belonging to two structural classes in genomes from the three kingdoms of life.

Authors:  Serge N Vinogradov; David Hoogewijs; Xavier Bailly; Raúl Arredondo-Peter; Michel Guertin; Julian Gough; Sylvia Dewilde; Luc Moens; Jacques R Vanfleteren
Journal:  Proc Natl Acad Sci U S A       Date:  2005-08-01       Impact factor: 11.205

6.  Purification and spectroscopic characterization of Ctb, a group III truncated hemoglobin implicated in oxygen metabolism in the food-borne pathogen Campylobacter jejuni.

Authors:  Laura M Wainwright; Yinghua Wang; Simon F Park; Syun-Ru Yeh; Robert K Poole
Journal:  Biochemistry       Date:  2006-05-16       Impact factor: 3.162

7.  Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.

Authors:  Julie A Hoy; Benoit J Smagghe; Puspita Halder; Mark S Hargrove
Journal:  Protein Sci       Date:  2007-02       Impact factor: 6.725

8.  Spectroscopic characterization of a truncated hemoglobin from the nitrogen-fixing bacterium Herbaspirillum seropedicae.

Authors:  Guilherme Razzera; Javier Vernal; Debora Baruh; Viviane I Serpa; Carolina Tavares; Flávio Lara; Emanuel M Souza; Fábio O Pedrosa; Fábio C L Almeida; Hernán Terenzi; Ana Paula Valente
Journal:  J Biol Inorg Chem       Date:  2008-06-12       Impact factor: 3.358

9.  Inducible defense mechanism against nitric oxide in Candida albicans.

Authors:  Breanna D Ullmann; Hadley Myers; Wiriya Chiranand; Anna L Lazzell; Qiang Zhao; Luis A Vega; Jose L Lopez-Ribot; Paul R Gardner; Michael C Gustin
Journal:  Eukaryot Cell       Date:  2004-06

10.  NsrR: a key regulator circumventing Salmonella enterica serovar Typhimurium oxidative and nitrosative stress in vitro and in IFN-gamma-stimulated J774.2 macrophages.

Authors:  Nicola J Gilberthorpe; Margaret E Lee; Tania M Stevanin; Robert C Read; Robert K Poole
Journal:  Microbiology (Reading)       Date:  2007-06       Impact factor: 2.777

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