THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBIN

The hemoglobin (VHb) from Vitreoscilla was the first bacterial hemoglobin discovered. Its structure and function have been extensively investigated, and engineering of a wide variety of heterologous organisms to express VHb has been performed to increase their growth and productivity. This strategy...

Full description

Bibliographic Details
Main Authors: Benjamin C. Stark, Kanak L. Dikshit, Krishna R. Pagilla
Format: Article
Language:English
Published: Elsevier 2012-10-01
Series:Computational and Structural Biotechnology Journal
Online Access:http://www.sciencedirect.com/science/article/pii/S2001037014600581
id doaj-1300b5fe89354be3b5def1ba498dcf08
record_format Article
spelling doaj-1300b5fe89354be3b5def1ba498dcf082020-11-24T23:00:41ZengElsevierComputational and Structural Biotechnology Journal2001-03702012-10-013410.5936/csbj.201210002THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBINBenjamin C. Stark0Kanak L. Dikshit1Krishna R. Pagilla2Biology Division, Department of Biological and Chemical Sciences, Illinois Institute of Technology, Chicago IL 60616, USAInstitute of Microbial Technology, Sec-39a, Chandigarh, 160036, IndiaDepartment of Civil and Architectural Engineering, Illinois Institute of Technology, Chicago IL 60616, USAThe hemoglobin (VHb) from Vitreoscilla was the first bacterial hemoglobin discovered. Its structure and function have been extensively investigated, and engineering of a wide variety of heterologous organisms to express VHb has been performed to increase their growth and productivity. This strategy has shown promise in applications as far-ranging as the production of antibiotics and petrochemical replacements by microorganisms to increasing stress tolerance in plants. These applications of “VHb technology” have generally been of the “black box” variety, wherein the endpoint studied is an increase in the levels of a certain product or improved growth and survival. Their eventual optimization, however, will require a thorough understanding of the various functions and activities of VHb, and how VHb expression ripples to affect metabolism more generally. Here we review the current knowledge of these topics. VHb's functions all involve oxygen binding (and often delivery) in one way or another. Several biochemical and structure-function studies have provided an insight into the molecular details of this binding and delivery. VHb activities are varied. They include supply of oxygen to oxygenases and the respiratory chain, particularly under low oxygen conditions; oxygen sensing and modulation of transcription factor activity; and detoxification of NO, and seem to require interactions of VHb with “partner proteins”. VHb expression affects the levels of ATP and NADH, although not enormously. VHb expression may affect the level of many compounds of intermediary metabolism, and, apparently, alters the levels of expression of many genes. Thus, the metabolic changes in organisms engineered to express VHb are likely to be numerous and complicated.http://www.sciencedirect.com/science/article/pii/S2001037014600581
collection DOAJ
language English
format Article
sources DOAJ
author Benjamin C. Stark
Kanak L. Dikshit
Krishna R. Pagilla
spellingShingle Benjamin C. Stark
Kanak L. Dikshit
Krishna R. Pagilla
THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBIN
Computational and Structural Biotechnology Journal
author_facet Benjamin C. Stark
Kanak L. Dikshit
Krishna R. Pagilla
author_sort Benjamin C. Stark
title THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBIN
title_short THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBIN
title_full THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBIN
title_fullStr THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBIN
title_full_unstemmed THE BIOCHEMISTRY OF VITREOSCILLA HEMOGLOBIN
title_sort biochemistry of vitreoscilla hemoglobin
publisher Elsevier
series Computational and Structural Biotechnology Journal
issn 2001-0370
publishDate 2012-10-01
description The hemoglobin (VHb) from Vitreoscilla was the first bacterial hemoglobin discovered. Its structure and function have been extensively investigated, and engineering of a wide variety of heterologous organisms to express VHb has been performed to increase their growth and productivity. This strategy has shown promise in applications as far-ranging as the production of antibiotics and petrochemical replacements by microorganisms to increasing stress tolerance in plants. These applications of “VHb technology” have generally been of the “black box” variety, wherein the endpoint studied is an increase in the levels of a certain product or improved growth and survival. Their eventual optimization, however, will require a thorough understanding of the various functions and activities of VHb, and how VHb expression ripples to affect metabolism more generally. Here we review the current knowledge of these topics. VHb's functions all involve oxygen binding (and often delivery) in one way or another. Several biochemical and structure-function studies have provided an insight into the molecular details of this binding and delivery. VHb activities are varied. They include supply of oxygen to oxygenases and the respiratory chain, particularly under low oxygen conditions; oxygen sensing and modulation of transcription factor activity; and detoxification of NO, and seem to require interactions of VHb with “partner proteins”. VHb expression affects the levels of ATP and NADH, although not enormously. VHb expression may affect the level of many compounds of intermediary metabolism, and, apparently, alters the levels of expression of many genes. Thus, the metabolic changes in organisms engineered to express VHb are likely to be numerous and complicated.
url http://www.sciencedirect.com/science/article/pii/S2001037014600581
work_keys_str_mv AT benjamincstark thebiochemistryofvitreoscillahemoglobin
AT kanakldikshit thebiochemistryofvitreoscillahemoglobin
AT krishnarpagilla thebiochemistryofvitreoscillahemoglobin
AT benjamincstark biochemistryofvitreoscillahemoglobin
AT kanakldikshit biochemistryofvitreoscillahemoglobin
AT krishnarpagilla biochemistryofvitreoscillahemoglobin
_version_ 1725641492483014656