TERMINAL OXIDATION SYSTEM IN BACTERIA: V. PRELIMINARY STUDY ON PHYSIOLOGICAL FUNCTION OF THE RESPIRATORY COMPONENTS OF PSEUDOMONAS AERUGINOSA
- 1 October 1959
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 46 (10), 1289-1301
- https://doi.org/10.1093/oxfordjournals.jbchem.a126924
Abstract
The opal glass method (cf.M.Calvin and K. Shibata, Biochim. Biophys. Acta, 17,1(1955)) was applied to the functioning cytochromes in the intact cells. The following electron-transport systems are proposed: (a) substrate (e. g., lactate) [forward arrow] diphosphopyridine nucleotide (DPHN)[forward arrow](by DPNH-P. cytochrome554 reductase)[forward arrow] P.cytochrome554 P. cytochrome 55 or P. blue protein [forward arrow] (by P. cytochrome oxidase (A2 type)) [forward arrow] 02; (b) Succinate[forward arrow](by succinic P. cytochrome560 reductase) [forward arrow] P. cytochrome560[long dash](main path)(by nitrate reductase)[forward arrow] NO3" or P. cytochromeseo560[long dash][long dash](side path)[forward arrow] P. cytochromeg551 or P. blue protein[forward arrow] 02. The exptl. results suggests the existence of possible electron transfer between P. cytochromes554 and 560. Those P. cytochromes are specific to P. cytochrome oxidase and cannot be linked to animal cytochrome a nor can they oxidize reduced cytochrome c of yeast or heart tissue.This publication has 11 references indexed in Scilit:
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