Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase.

Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Abstract Text:

To probe the location of the quinol oxidation site and physical interactions for inter-subunit electron transfer, we constructed and characterized two chimeric oxidases in which subunit II (CyoA) of cytochrome bo-type ubiquinol oxidase from Escherichia coli was replaced with the counterpart (CaaA) of caa(3)-type cytochrome c oxidase from thermophilic Bacillus PS3. In pHNchi5, the C-terminal hydrophilic domain except a connecting region as to transmembrane helix II of CyoA was replaced with the counterpart of CaaA, which carries the Cu(A) site and cytochrome c domain. The resultant chimeric oxidase was detected immunochemically and spectroscopically, and the turnover numbers for Q(1)H(2) (ubiquinol-1) and TMPD (N,N, N',N'-tetramethyl-p-phenylenediamine) oxidation were 28 and 8.5 s(-1), respectively. In pHNchi6, the chimeric oxidase was designed to carry a minimal region of the cupredoxin fold containing all the Cu(A) ligands, and showed enzymatic activities of 65 and 5.1 s(-1), and an expression level better than that of pHNchi5. Kinetic analyses proved that the apparent lower turnover of the chimeric enzyme by pHNchi6 was due to the higher K(m) of the enzyme for Q(1)H(2) (220 microM) than that of cytochrome bo (48 microM), while in the enzyme by pHNchi5, both substrate-binding and internal electron transfer were perturbed. These results suggest that the connecting region and the C-terminal alpha(1)-alpha(2)-beta(11)-alpha(3) domain of CyoA are involved in the quinol oxidation and/or physical interactions for inter-subunit electron transfer, supporting our previous proposal [Sato-Watanabe, M., Mogi, T., Miyoshi, H., and Anraku, Y. (1998) Biochemistry 37, 12744-12752]. The close relationship of E. coli quinol oxidases to cytochrome c oxidase of Gram-positive bacteria like Bacillus was also indicated.

Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Publishing Authors By Initials

For similar genetic processes: recombination, genetic: transformation, genetic research abstracts see: genetic processes: recombination, genetic: transformation, genetic research

PUBMED ID PMID:

MEDLINE DATE:

Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 126

Page Numbers: 934-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1999

Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Keywords Mesh Terms:

KEYWORDS: Transformation, Genetic

MESH TERMS: metabolism

Chemical & Substance for Abstract: Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Information

Substance Name: Electron Transport Complex IV

Registry Number: EC 1.9.3.1

Grant and Affiliation Information for Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase.

AFFILIATION: Department of Biochemical Engineering and Science, Kyusyu Institute of Technology, Iizuka, Fukuoka, 820-8502, Japan.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa3-type cytochrome c oxidase Related Publications

• A novel cytochrome b(o/a)3-type oxidase from Bacillus stearothermophilus catalyzes cytochrome c-551 oxidation.
• Acute myocardial infarction caused by spontaneous postpartum coronary artery dissection.
• Binaural perception of the modulation depth of AM signals.
• CT findings and progression of small peripheral lung neoplasms having a replacement growth pattern.
• Characterization of a cb-type cytochrome c oxidase from Helicobacter pylori.
• Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain.
• Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase.
• Effect of dipyridamole on the blood flow in coronary aneurysms resulting from Kawasaki disease.
• Effects of the photosynthetic inhibitors on the respiration of yeast mitochondria.
• Expression of the Escherichia coli bo-type ubiquinol oxidase with a chimeric subunit II having the CuA-cytochrome c domain from the thermophilic Bacillus caa3-type cytochrome c oxidase.
• Follistatin Suppresses the Production of Experimental Multiple-Organ Metastasis by Small Cell Lung Cancer Cells in Natural Killer Cell-Depleted SCID Mice.
• Importance of hydrophobic interaction between a SoxB-type cytochrome c oxidase with its natural substrate cytochrome c-551 and its mutants.
• Intra- and inter-complex cross-linking of subunits in the quinol oxidase super-complex from thermophilic Bacillus PS3.
• Isolation of a novel menaquinone with a partly hydrogenated side chain from Propionibacterium arabinosum.
• Measurement of proton pump activity of the thermophilic bacterium PS3 and Nitrobacter agilis at the cytochrome oxidase level using total membrane and heptyl thioglucoside.
• Nucleotide sequence of the gene coding for four subunits of cytochrome c oxidase from the thermophilic bacterium PS3.
• Observations on the occurrence of exacerbations in clinical course of systemic lupus erythematosus.
• Occurrence of cobalt coproporphyrin in Propionibacterium arabinosum.
• Preparation and characterization of the hydrophilic CuA-cytochrome c domain of subunit II of cytochrome c oxidase from thermophilic bacillus PS3.
• Purification and characterization of cytochrome c-553 from Helicobacter pylori.
• Rhizopus delemar is the proper name for Rhizopus oryzae fumaric-malic acid producers.
• Role of alpha1-acid glycoprotein in therapeutic antifibrotic effects of imatinib with macrolides in mice.
• The redox reactions in propionic acid fermantation. I. Occurrence and nature of an electron transfer system in Propionibacterium arabinosum.
• The redox reactions in propionic acid fermentation. 3. Enzymatic properties of NAD-independent glycerol-phosphate dehydrogenase from Propionibacterium arabinosum.
• The redox reactions in propionic acid fermentation. IV. Participation of menaquinone in the electron transfer system in Propionibacterium arabinosum.
• The therapeutic efficacy of anti vascular endothelial growth factor antibody, bevacizumab, and pemetrexed against orthotopically implanted human pleural mesothelioma cells in severe combined immunodeficient mice.
• [Congenital aortic valve stenosis in an infant]
• [Lumbar: DXA(QDR, DPX, XR)]
• [Modulation of central sudomotor control by short-term heat acclimation as evidenced by frequency of sweat expulsions]
• [Respiratory science and clinic to meet social needs]