Chimeric Vitreoscilla Hemoglobin (VHb) Carrying a Flavoreductase Domain Relieves Nitrosative Stress in Escherichia coli: New Insight into the Functional Role of VHb

Dimeric hemoglobin (VHb) from the bacterium Vitreoscilla sp. strain C1 displays 30 to 53% sequence identity with the heme-binding domain of flavohemoglobins (flavoHbs) and exhibits the presence of potential sites for the interaction with its FAD/NADH reductase partner. The intersubunit contact regio...

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Bibliografiske detaljer
Main Authors:	Kaur, Ramandeep, Pathania, Ranjana, Sharma, Vishwamitra, Mande, Shekhar C., Dikshit, Kanak L.
Format:	Artigo
Sprog:	Inglês
Udgivet:	American Society for Microbiology 2002
Fag:	Physiology and Biotechnology
Online adgang:	https://ncbi.nlm.nih.gov/pmc/articles/PMC126558/ https://ncbi.nlm.nih.gov/pubmed/11772621 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.68.1.152-160.2002
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Chimeric Vitreoscilla Hemoglobin (VHb) Carrying a Flavoreductase Domain Relieves Nitrosative Stress in Escherichia coli: New Insight into the Functional Role of VHb

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