HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Webster, D. A. Articles by Liu, C. Y. Search for Related Content PubMed PubMed Citation Articles by Webster, D. A. Articles by Liu, C. Y. Social Bookmarking                      What's this?

Reduced Nicotinamide Adenine Dinucleotide Cytochrome o Reductase Associated with Cytochrome o Purified from Vitreoscilla

EVIDENCE FOR AN INTERMEDIATE OXYGENATED FORM OF CYTOCHROME o

From the ¹ From the Department of Biology, Illinois Institute of Technology, Chicago, Illinois 60616

Cytochrome o, purified from Vitreoscilla sp., Murray strain 389, has a carbon monoxide difference spectrum with absorption maxima at 569, 535, and 419 nm. This spectrum resembles closely the carbon monoxide difference spectrum of whole cell suspensions of Vitreoscilla. The reduction of cytochrome o by NADH is catalyzed by a component(s) present in purified preparations of the cytochrome, and this NADH-cytochrome o reductase activity could be assayed in these preparations aerobically by following the absorbancy increase at 420 nm on the addition of NADH. Aerobic difference spectra of cytochrome o solutions, (NADH) minus (untreated), have absorption maxima at 577, 544, and 420 nm, and this spectrum is believed to represent the formation of an "oxygenated" form of reduced cytochrome o. Difference spectra of cytochrome o, that has been chemically reduced by excess sodium dithionite, have absorption maxima at 560 and 435 nm, which presumably are the absorption maxima characteristic of the reduced, but not oxygenated, form of cytochrome o. Chromatography of cytochrome o on Sephadex G-100 and DEAE-cellulose resulted in purification of cytochrome o and NADH-cytochrome o reductase, but separation of the reductase activity from the cytochrome was not achieved. Reductase activity with cytochrome o as acceptor was separated chromatographically from reductase activity with 2,6-dichlorophenolindophenol as acceptor. Oxygen uptake of purified fractions on the addition of NADH was associated primarily with NADH-cytochrome o reductase activity.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. D. Frey, J. Farres, C. J. T. Bollinger, and P. T. Kallio Bacterial Hemoglobins and Flavohemoglobins for Alleviation of Nitrosative Stress in Escherichia coli Appl. Envir. Microbiol., October 1, 2002; 68(10): 4835 - 4840. [Abstract] [Full Text] [PDF]

				A. D. Frey, J. Fiaux, T. Szyperski, K. Wüthrich, J. E. Bailey, and P. T. Kallio Dissection of Central Carbon Metabolism of Hemoglobin-Expressing Escherichia coli by 13C Nuclear Magnetic Resonance Flux Distribution Analysis in Microaerobic Bioprocesses Appl. Envir. Microbiol., February 1, 2001; 67(2): 680 - 687. [Abstract] [Full Text]

				A. D. Frey, J. E. Bailey, and P. T. Kallio Expression of Alcaligenes eutrophus Flavohemoprotein and Engineered Vitreoscilla Hemoglobin-Reductase Fusion Protein for Improved Hypoxic Growth of Escherichia coli Appl. Envir. Microbiol., January 1, 2000; 66(1): 98 - 104. [Abstract] [Full Text]

				M. Joshi, S. Mande, and K. L. Dikshit Hemoglobin Biosynthesis in Vitreoscilla stercoraria DW: Cloning, Expression, and Characterization of a New Homolog of a Bacterial Globin Gene Appl. Envir. Microbiol., June 1, 1998; 64(6): 2220 - 2228. [Abstract] [Full Text]