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Plant hemoglobins can be maintained in functional form by reduced flavins in the nuclei and confer differential tolerance to nitro-oxidative stress.
MedLine Citation:
PMID:  24118423     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Bacteria, plant and animal hemoglobins (Hbs) need to have their hemes in the ferrous state to bind O2 and other physiological ligands. Here we have characterized the full set of nonsymbiotic (class 1 and 2) and 'truncated' (class 3) Hbs of Lotus japonicus. Class 1 Hbs are hexacoordinate but class 2 and 3 Hbs are pentacoordinate. Three globins, Glb1-1, Glb2 and Glb3-1, are nodule-enhanced proteins. The O2 affinity of Glb1-1 (~50 pM) was the highest known for any Hb and the protein may function as an O2 scavenger. The five globins were reduced by free flavins, which transfer electrons from NAD(P)H to the heme iron in aerobic and anaerobic conditions. Class 1 Hbs were reduced at very fast rates with FAD, class 2 Hbs at slower rates with both FMN and FAD, and class 3 Hbs at intermediate rates with FMN. The three globin classes were immunolocalized predominantly in the nuclei. Flavins were quantified in legume nodules and nuclei and their concentrations were sufficient to maintain Hbs in their functional state. All Hbs, except Glb1-1, could be expressed in a flavohemoglobin-deficient yeast mutant and found to confer tolerance to oxidative stress induced by methyl viologen, copper or low temperature, indicating an antioxidative role of the hemes. However, only Glb1-2 and Glb2 afforded protection from nitrosative stress induced by S-nitrosoglutathione. Because this compound is specifically involved in transnitrosation reactions with thiol groups, our results point to a contribution of the single cysteine residues of the proteins in the stress response. This article is protected by copyright. All rights reserved.
Authors:
Martha Sainz; Carmen Pérez-Rontomé; Javier Ramos; Jose Miguel Mulet; Euan K James; Ujjal Bhattacharjee; Jacob W Petrich; Manuel Becana
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-10-9
Journal Detail:
Title:  The Plant journal : for cell and molecular biology     Volume:  -     ISSN:  1365-313X     ISO Abbreviation:  Plant J.     Publication Date:  2013 Oct 
Date Detail:
Created Date:  2013-10-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9207397     Medline TA:  Plant J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
This article is protected by copyright. All rights reserved.
Affiliation:
Departamento de Nutrición Vegetal, Estación Experimental de Aula Dei, Consejo Superior de Investigaciones Científicas (CSIC), Apartado 13034, 50080, Zaragoza, Spain.
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