Structure of CuB in the Binuclear Heme-Copper Center of the Cytochrome aa3-Type Quinol Oxidase from Bacillus subtilis: An ENDOR and EXAFS Study

Biochemistry ◽  
1995 ◽  
Vol 34 (32) ◽  
pp. 10245-10255 ◽  
Author(s):  
Yang C. Fann ◽  
Ishak Ahmed ◽  
Ninian J. Blackburn ◽  
John S. Boswell ◽  
Marina L. Verkhovskaya ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Cytochrome Aa3 ◽  
Quinol Oxidase ◽  
Copper Center ◽  
Exafs Study

scholarly journals High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes

1995 ◽  
Vol 309 (1) ◽  
pp. 279-283 ◽  
Author(s):  
W Henning ◽  
L Vo ◽  
J Albanese ◽  
B C Hill
Keyword(s):  
Bacillus Subtilis ◽  
Plasma Membranes ◽  
Sequence Data ◽  
High Yield ◽  
Cytochrome Aa3 ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Aerobic Culture ◽  
Conventional Procedure ◽  
Molecular Masses

When grown in aerated shaking culture, Bacillus subtilis expresses two different haem A-containing terminal oxidases: cytochrome aa3-quinol oxidase and cytochrome caa3 oxidase. This paper describes a high-yield conventional procedure for purifying the two haem A-containing oxidases from the same aerobic culture of Bacillus subtilis. Yields of close to 40% of the total haem A are achieved and about 6 mg of each of the purified oxidases is obtained from 4 litres of liquid culture. Both of the purified enzymes have two subunits, with apparent molecular masses of 71.6 kDa and 34.3 kDa for the cytochrome caa3 oxidase, and 67.6 kDa and 37.2 kDa for aa3-quinol oxidase. These features are in agreement with the sequence data for the corresponding structural genes in the aa3 and caa3 operons of B. subtilis. Some spectral and enzymic features of the two purified oxidases are reported that are consistent with the inclusion of both of these enzymes as members of the cytochrome oxidase superfamily.

Plasticity in the High Affinity Menaquinone Binding Site of the Cytochrome aa3-600 Menaquinol Oxidase from Bacillus subtilis

Biochemistry ◽  
2015 ◽  
Vol 54 (32) ◽  
pp. 5030-5044 ◽  
Author(s):  
Sophia M. Yi ◽  
Alexander T. Taguchi ◽  
Rimma I. Samoilova ◽  
Patrick J. O’Malley ◽  
Robert B. Gennis ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Binding Site ◽  
Cytochrome Aa3 ◽  
High Affinity

scholarly journals Functional analysis of subunits III and IV of Bacillus subtilis aa3-600 quinol oxidase by in vitro mutagenesis and gene replacement

1995 ◽  
Vol 1232 (1-2) ◽  
pp. 67-74 ◽  
Author(s):  
Gaetano Villani ◽  
Maria Tattoli ◽  
Nazzareno Capitanio ◽  
Philippe Glaser ◽  
Sergio Papa ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Bacillus Subtilis ◽  
Gene Replacement ◽  
In Vitro Mutagenesis ◽  
Quinol Oxidase

scholarly journals A cytochrome aa3-type quinol oxidase from Desulfurolobus ambivalens, the most acidophilic archaeon

1994 ◽  
Vol 117 (3) ◽  
pp. 275-280 ◽  
Author(s):  
S. Anemüller ◽  
C.L. Schmidt ◽  
I. Pacheco ◽  
G. Schäfer ◽  
M. Teixeira
Keyword(s):  
Cytochrome Aa3 ◽  
Quinol Oxidase

scholarly journals Terminal Oxidases of Bacillus subtilisStrain 168: One Quinol Oxidase, Cytochromeaa3 or Cytochrome bd, Is Required for Aerobic Growth

2000 ◽  
Vol 182 (23) ◽  
pp. 6557-6564 ◽  
Author(s):  
Lena Winstedt ◽  
Claes von Wachenfeldt
Keyword(s):  
Bacillus Subtilis ◽  
Sequence Analysis ◽  
Terminal Oxidase ◽  
Rich Medium ◽  
Aerobic Growth ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Cytochrome Bd ◽  
Heme Copper Oxidases ◽  
Quinol Oxidases

ABSTRACT The gram-positive endospore-forming bacterium Bacillus subtilis has, under aerobic conditions, a branched respiratory system comprising one quinol oxidase branch and one cytochrome oxidase branch. The system terminates in one of four alternative terminal oxidases. Cytochrome caa 3 is a cytochromec oxidase, whereas cytochrome bd and cytochromeaa 3 are quinol oxidases. A fourth terminal oxidase, YthAB, is a putative quinol oxidase predicted from DNA sequence analysis. None of the terminal oxidases are, by themselves, essential for growth. However, one quinol oxidase (cytochromeaa 3 or cytochrome bd) is required for aerobic growth of B. subtilis strain 168. Data indicating that cytochrome aa 3 is the major oxidase used by exponentially growing cells in minimal and rich medium are presented. We show that one of the two heme-copper oxidases, cytochrome caa 3 or cytochromeaa 3, is required for efficient sporulation ofB. subtilis strain 168 and that deletion of YthAB in a strain lacking cytochrome aa 3 makes the strain sporulation deficient.

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