Biomaterial Database

Cross-talk between mitochondrial malate dehydrogenase and the cytochrome bc1 complex. 2010

Qiyu Wang, and Linda Yu, and Chang-An Yu

Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma 74078, USA.

The interactions between the mitochondrial cytochrome bc(1) complex and matrix-soluble proteins were studied by a precipitation pulldown technique. Purified, detergent-dispersed bc(1) complex was incubated with mitochondrial matrix proteins followed by dialysis in the absence of detergent. The interacting protein(s) was co-precipitated with bc(1) complex upon centrifugation. One of the matrix proteins pulled down by bc(1) complex was identified as mitochondrial malate dehydrogenase (MDH) by matrix-assisted laser desorption ionization time-of-flight mass spectrometry and confirmed by Western blotting with anti-MDH antibody. Using a cross-linking technique, subunits I, II (core I and II), and V of the bc(1) complex were identified as the interacting sites for MDH. Incubating purified MDH with the detergent dispersed bc(1) complex results in an increase of the activities of both the bc(1) complex and MDH. The effect of the bc(1) complex on the activities of MDH is unidirectional (oxaloacetate --> malate). These results suggest that the novel cross-talk between citric acid cycle enzymes and electron transfer chain complexes might play a regulatory role in mitochondrial bioenergetics.

UI	MeSH Term	Description	Entries
D008291	Malate Dehydrogenase	An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.	Malic Dehydrogenase,NAD-Malate Dehydrogenase,Dehydrogenase, Malate,Dehydrogenase, Malic,Dehydrogenase, NAD-Malate,NAD Malate Dehydrogenase
D008929	Mitochondria, Heart	The mitochondria of the myocardium.	Heart Mitochondria,Myocardial Mitochondria,Mitochondrion, Heart,Heart Mitochondrion,Mitochondria, Myocardial
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D002417	Cattle	Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.	Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D003432	Cross-Linking Reagents	Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.	Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D004579	Electron Transport	The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)	Respiratory Chain,Chain, Respiratory,Chains, Respiratory,Respiratory Chains,Transport, Electron
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D014450	Electron Transport Complex III	A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.	Complex III,Cytochrome bc1 Complex,Ubiquinol-Cytochrome-c Reductase,Coenzyme Q-Cytochrome-c Reductase,Coenzyme QH2-Cytochrome-c Reductase,Core I Protein, UCCreductase,Core I Protein, Ubiquinol-Cytochrome c Reductase,Core II Protein, UCCreductase,Core II Protein, Ubiquinol-Cytochrome c Reductase,Cytochrome b-c2 Oxidoreductase,Cytochrome bc1,Dihydroubiquinone-Cytochrome-c Reductase,QH(2)-Cytochrome-c Reductase,QH(2)-Ferricytochrome-c Oxidoreductase,Ubihydroquinone-Cytochrome-c Reductase,Ubiquinol-Cytochrome c Reductase,Ubiquinone-Cytochrome b-c2 Oxidoreductase,Coenzyme Q Cytochrome c Reductase,Coenzyme QH2 Cytochrome c Reductase,Core I Protein, Ubiquinol Cytochrome c Reductase,Core II Protein, Ubiquinol Cytochrome c Reductase,Cytochrome b c2 Oxidoreductase,Dihydroubiquinone Cytochrome c Reductase,Reductase, Ubiquinol-Cytochrome c,Ubihydroquinone Cytochrome c Reductase,Ubiquinol Cytochrome c Reductase,Ubiquinone Cytochrome b c2 Oxidoreductase
D015153	Blotting, Western	Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.	Immunoblotting, Western,Western Blotting,Western Immunoblotting,Blot, Western,Immunoblot, Western,Western Blot,Western Immunoblot,Blots, Western,Blottings, Western,Immunoblots, Western,Immunoblottings, Western,Western Blots,Western Blottings,Western Immunoblots,Western Immunoblottings
D019032	Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization	A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.	Laser Desorption-Ionization Mass Spectrometry, Matrix-Assisted,MALD-MS,MALDI,Mass Spectrometry, Matrix-Assisted Laser Desorption-Ionization,Mass Spectroscopy, Matrix-Assisted Laser Desorption-Ionization,Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry,Spectroscopy, Mass, Matrix-Assisted Laser Desorption-Ionization,MALDI-MS,MS-MALD,SELDI-TOF-MS,Surface Enhanced Laser Desorption Ionization Mass Spectrometry,Laser Desorption Ionization Mass Spectrometry, Matrix Assisted,MALDI MS,Mass Spectrometry, Matrix Assisted Laser Desorption Ionization,Mass Spectroscopy, Matrix Assisted Laser Desorption Ionization,Matrix Assisted Laser Desorption Ionization Mass Spectrometry