Purification and properties of NADH dehydrogenase from an alkalophilic bacillus

Hisae, Nobuo; Koyama, Noriyuki; Sekiguchi, Toshio; Nosoh, Yoshiaki

doi:10.1016/0167-4838(83)90219-4

Cited by 25 publications

(14 citation statements)

References 30 publications

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“…Membrane-bound NADH dehydrogenase was purified from alkalophilic Bacillus YN-1 to electrophoretical homogeneity, as reported previously (12).…”

Section: Methodsmentioning

confidence: 99%

“…Membrane-bound NADH dehydrogenase [EC 1.6.99 .3] have been purified from many microorganisms (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14). The enzyme are flavoproteins containing FAD or FMN as prosthetic group.…”

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confidence: 99%

“…The subunit structures of microbial NADH dehydrogenases, however, have been revealed with only the following enzymes. The enzyme from Bacillus stearothermophilus is monomeric (6) and that from alkalophilic Bacillus dimeric (12). Each of the two subunits (65 kDa) of the alkalophile enzyme contains the catalytic and liposome-binding regions (15).…”

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confidence: 99%

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Tryptic Digestion of NADH Dehydrogenase from Alkalophilic Bacillus1

Kanaya

Koyama

et al. 1989

The Journal of Biochemistry

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The alkalophile NADH dehydrogenase (NADH: 2,6-dichlorophenolindophenol oxidoreductase) [EC 1.6.99.3] consists of two identical subunits of 65 kDa, and each subunit contains the catalytic and liposome-binding regions. On treatment with trypsin, the polypeptide exhibiting the liposome-binding property in one of the subunits was digested to form an enzymatically active hetero-dimer (40 and 65 kDa), and then the polypeptide in the other subunit was digested to form an active homo-dimer (40 and 40 kDa). The hetero-dimer bound to liposomes, but the homo-dimer did not. Kinetic analysis showed that removal of one or two of the polypeptides in the enzyme slightly affects its kinetic parameters. For all the enzyme species, NAD inhibited competitively with respect to NADH and non-competitively with respect to 2,6-dichlorophenolindophenol. The partially determined amino acid sequence of this alkalophile enzyme suggested that (i) a long random-coiled peptide (58 amino acid residues) or a portion of the peptide is located between the polypeptides with liposome-binding and catalytic properties, (ii) the polypeptide exhibiting liposome-binding property is in the amino terminal region of the enzyme, (iii) the amino acid sequences around the subtilisin and trypsin cleavage sites of the peptide are hydrophilic and on the surface of the protein molecule and therefore are susceptible to digestion, and (iv) the FAD-binding site is located near the amino terminal region of the catalytic region.

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“…Membrane-bound NADH dehydrogenase was purified from alkalophilic Bacillus YN-1 to electrophoretical homogeneity, as reported previously (12).…”

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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Tryptic Digestion of NADH Dehydrogenase from Alkalophilic Bacillus1

Kanaya

Koyama

et al. 1989

The Journal of Biochemistry

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“…B. clarkii DSM 8720 T exhibited a ratio of 6.0. It has been reported that NADH dehydrogenases in Gram-positive bacteria do not translocate protons (Hisae et al 1983;Xu et al 1991;Liu et al 2008 …”

Section: H + /O Ratiomentioning

confidence: 99%

Relationship between rates of respiratory proton extrusion and ATP synthesis in obligately alkaliphilic Bacillus clarkii DSM 8720T

Hirabayashi

Goto

Morimoto

et al. 2012

J Bioenerg Biomembr

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“…Examples of such enzymes have been isolated from a variety of bacteria, including E. coli (63), Bacillus sp. strain YN-1 (24,56), and T. thermophilus (61).…”

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Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant

1993

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The ndhF gene of the unicellular marine cyanobacterium Synechococcus sp. strain PCC 7002 was cloned and characterized. NdhF is a subunit of the type 1, multisubunit NADH:plastoquinone oxidoreductase (NADH dehydrogenase). The nucleotide sequence of the gene predicts an extremely hydrophobic protein of 664 amino acids with a calculated mass of 72.9 kDa. The ndhF gene was shown to be single copy and transcribed into a monocistronic mRNA of 2,300 nucleotides. An ndhF null mutation was successfully constructed by interposon mutagenesis, demonstrating that NdhF is not required for cell viability under photoautotrophic growth conditions. The mutant strain exhibited a negligible rate of oxygen uptake in the dark, but its photosynthetic properties (oxygen evolution, chlorophyll/P700 ratio, and chlorophyll/P680 ratio) were generally similar to those of the wild type. Although the ndhF mutant strain grew as rapidly as the wild-type strain at high light intensity, the mutant grew more slowly than the wild type at lower light intensities and did not grow at all under photoheterotrophic conditions. The roles of the NADH:plastoquinone oxidoreductase in photosynthetic and respiratory electron transport are discussed.During respiration in mitochondria, NADH is oxidized and electrons are passed through a series of membranebound oxidoreductase complexes to oxygen. These enzymes combine electron transfer reactions to the vectoral translocation of protons across the inner mitochondrial membrane, thereby generating a proton motive force which can be used for ATP synthesis or other energy-requiring processes (55). The first major enzyme complex (complex I) in this chain is NADH:ubiquinone oxidoreductase (EC 1.6.99.3, also referred to as NADH dehydrogenase; for recent reviews, see references 16, 53, and 55). This mitochondrial enzyme comprises more than 40 subunits, and recently the primary structures of all known components of the bovine complex have been determined (2,4,5,16,53,54). Although some of these subunits are encoded in the mitochondrial genome, the majority of them are encoded in the nucleus and must be imported into the mitochondria and assembled in the inner membrane (16,53,55).A surprising finding from analyses of the complete nucleotide sequences of the chloroplast genomes of liverwort (40), tobacco (48), and rice (23) is that these genomes contain 11 genes with sequence similarity to components of the mitochondrial NADH dehydrogenase. Although it is known that these genes are transcribed (29), the protein products of the chloroplast ndh genes and the putative NADH dehydrogenase which they would form have not yet been identified. Sporadic reports concerning the occurrence of a respiratory chain in the chloroplasts of algae and higher plants have appeared (7,21,31,41); however, the role of such an electron transport chain in chloroplast function is not well understood at present.Several procaryotes have been shown to possess two types of NADH dehydrogenases, only one of which is coupled to proton translocation (60). The ...

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Purification and properties of NADH dehydrogenase from an alkalophilic bacillus

Cited by 25 publications

References 30 publications

Tryptic Digestion of NADH Dehydrogenase from Alkalophilic Bacillus1

Tryptic Digestion of NADH Dehydrogenase from Alkalophilic Bacillus1

Relationship between rates of respiratory proton extrusion and ATP synthesis in obligately alkaliphilic Bacillus clarkii DSM 8720T

Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant

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