NDLI: The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant.

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The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ban, Bhupal Li, Ting-feng Painter, Richard G. Blake, Robert C.
Description	Author Affiliation: Li TF ( From the College of Pharmacy, Xavier University of Louisiana, New Orleans, Louisiana 70125.); Painter RG ( From the College of Pharmacy, Xavier University of Louisiana, New Orleans, Louisiana 70125.); Ban B ( From the College of Pharmacy, Xavier University of Louisiana, New Orleans, Louisiana 70125.); Blake RC ( From the College of Pharmacy, Xavier University of Louisiana, New Orleans, Louisiana 70125 rblake@xula.edu.)
Abstract	Electron transfer reactions among three prominent colored proteins in intact cells of Acidithiobacillus ferrooxidans were monitored using an integrating cavity absorption meter that permitted the acquisition of accurate absorbance data in suspensions of cells that scattered light. The concentrations of proteins in the periplasmic space were estimated to be 350 and 25 mg/ml for rusticyanin and cytochrome c, respectively; cytochrome a was present as one molecule for every 91 nm(2) in the cytoplasmic membrane. All three proteins were rapidly reduced to the same relative extent when suspensions of live bacteria were mixed with different concentrations of ferrous ions at pH 1.5. The subsequent molecular oxygen-dependent oxidation of the multicenter respiratory chain occurred with a single macroscopic rate constant, regardless of the proteins' in vitro redox potentials or their putative positions in the aerobic iron respiratory chain. The crowded electron transport proteins in the periplasm of the organism constituted an electron conductive medium where the network of protein interactions functioned in a concerted fashion as a single ensemble with a standard reduction potential of 650 mV. The appearance of product ferric ions was correlated with the reduction levels of the periplasmic electron transfer proteins; the limiting first-order catalytic rate constant for aerobic respiration on iron was 7,400 s(-1). The ability to conduct direct spectrophotometric studies under noninvasive physiological conditions represents a new and powerful approach to examine the extent and rates of biological events in situ without disrupting the complexity of the live cellular environment.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	30
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-07-24
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acidithiobacillus Metabolism Electron Transport Oxidation-Reduction Chemistry Aerobiosis Cytochromes a Cytochromes c Kinetics Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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