12 research outputs found
Thiol Enzymes Protecting Mitochondria Against Oxidative Damage
No full text[No abstract available]348260270Boveris, A., Chance, B., Oshino, N., (1972) Biochem. J., 128, p. 617Kowaltowski, A.J., Vercesi, A.E., (2000) Mitochondria in Pathogenisis, p. 281. , J. J. Lemasters, and A.-L. Nieminen, eds., Plenum, New YorkTyler, D.D., (1975) Biochim. Biophys. Acta, 396, p. 335Zoratti, M., Szabò, I., (1995) Biochim. Biophys. Acta, 1241, p. 139Marchetti, P., Decaudin, D., Macho, A., Zamzami, N., Hirsch, T., Susin, S.A., Kroemer, G., (1997) Eur. J. Lmmunol., 27, p. 289Nomura, K., Imai, H., Koumura, T., Arai, M., Nakagawa, Y., (1999) J. Biol. Chem., 274, p. 29294Wullner, U., Seyfried, J., Groscurth, P., Beinroth, S., Winter, S., Gleichmann, M., Heneka, M., Klockgether, T., (1999) Brain Res., 826, p. 53Green, R.C., O'Brien, P.J., (1970) Biochim. Biophys. Acta, 197, p. 31Castilho, R.F., Kowaltowski, A.J., Vercesi, A.E., (1996) J. Bioenerg. Biomembr., 28, p. 523Dhanbhoora, C.M., Babson, J.R., (1992) Arch. Biochem. Biophys., 293, p. 130Tamura, T., McMicken, H.W., Smith, C.V., Hansen, T.N., (1996) Biochem. Biophys. Res. Commun., 222, p. 659Esworthy, R.S., Ho, Y.S., Chu, F.F., (1997) Arch. Biochem. Biophys., 340, p. 59Meister, A., (1995) Biochim. Biophys. Acta, 1271, p. 35Olafsdottir, K., Reed, D.J., (1988) Biochim. Biophys. Acta, 964, p. 377Radi, R., Turrens, J.F., Chang, L.Y., Bush, K.M., Crapo, J.D., Freeman, B.A., (1991) J. Biol. Chem., 266, p. 22028Kim, K., Kim, I.H., Lee, K.Y., Rhee, S.G., Stadtman, E.R., (1988) J. Biol. Chem., 263, p. 4704Chae, H.Z., Kim, I.H., Kim, K., Rhee, S.G., (1993) J. Biol. Chem., 268, p. 16815Netto, L.E.S., Chae, H.Z., Kang, S.W., Rhee, S.G., Stadtman, E.R., (1996) J. Biol. Chem., 271, p. 15315Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G., Rhee, S.G., (1994) Proc. Natl. Acad. Sci. U.S.A., 91, p. 7017Lim, Y.S., Cha, M.K., Kim, H.K., Kim, I.H., (1994) Gene, 140, p. 279Watabe, S., Hiroi, T., Yamamoto, Y., Fujioka, Y., Hasegawa, H., Yago, N., Takahashi, S.Y., (1997) Eur. J. Biochem., 249, p. 52Pedrajas, J.R., Miranda-Vizuete, A., Javanmardy, N., Gustafsson, J.A., Spyrou, G., (2000) J. Biol. Chem., 275, p. 16296Watabe, S., Hasegawa, H., Takimoto, K., Yamamoto, Y., Takahashi, S.Y., (1995) Biochem. Biophys. Res. Commun., 213, p. 1010Zhang, P., Liu, B., Kang, S.W., Seo, M.S., Rhee, S.G., Obeid, L.M., (1997) J. Biol. Chem., 272, p. 30615Kowaltowski, A.J., Netto, L.E.S., Vercesi, A.E., (1998) J. Biol. Chem., 273, p. 12766Kowaltowski, A.J., Vercesi, A.E., Rhee, S.G., Netto, L.E.S., (2000) FEBS Lett., 473, p. 177Chae, H.Z., Chung, S.J., Rhee, S.G., (1994) J. Biol. Chem., 269, p. 27670Stadtman, T.C., (2000) Ann. N. Y. Acad. Sci., 899, p. 399Mustacich, D., Powis, G., (2000) Biochem. J., 346, p. 1Moskovitz, J., Flescher, E., Berlett, B.S., Azare, J., Poston, J.M., Stadtman, E.R., (1998) Proc. Natl. Acad. Sci. U.S.A., 95, p. 14071Ursini, E., Maiorino, M., Gregolin, C., (1985) Biochim. Biophys. Acta, 839, p. 62Mickelson, J.R., Greaser, M.L., Marsh, B.B., (1980) Anal. Biochem., 109, p. 255Ellman, G.L., (1959) Arch. Biochem. Biophys., 82, p. 70Mar, T., (1981) J. Biochem. Biophys. Methods, 4, p. 177Garlid, K.D., Beavis, A.D., (1985) J. Biol. Chem., 260, p. 13434Fiskum, G., Craig, S.W., Decker, G.L., Lehninger, A.L., (1980) Proc. Natl. Acad. Sci. U.S.A., 77, p. 3430Fiskum, G., Kowaltowski, A.J., Andreyev, A.Y., Kushnareva, Y.E., Starkov, A.A., (2000) Methods Enzymol., 322, p. 222Docampo, R., Vercesi, A.E., (1989) J. Biol. Chem., 264, p. 108Nicholls, P., (1962) Biochim. Biophys. Acta., 59, p. 414Akerman, K.E., Wikström, M.K., (1976) FEBS Lett., 68, p. 191Vercesi, A.E., Bernardes, C.F., Hoffmann, M.E., Gadelha, F.R., Docampo, R., (1991) J. Biol. Chem., 266, p. 14431Jung, D.W., Bradshaw, P.C., Pfeiffer, D.R., (1997) J. Biol. Chem., 272, p. 2110
The Thiol-specific Antioxidant Enzyme Prevents Mitochondrial Permeability Transition: Evidence For The Participation Of Reactive Oxygen Species In This Mechanism
No full textMitochondrial swelling and membrane protein thiol oxidation associated with mitochondrial permeability transition induced by Ca2+ and inorganic phosphate are inhibited in a dose-dependent manner either by catalase, the thiol-specific antioxidant enzyme (TSA), a protein recently demonstrated to present thiol peroxidase activity, or ebselen, a selenium-containing heterocycle which also possesses thiol peroxidase activity. This inhibition of mitochondrial permeability transition is due to the removal of mitochondrial-generated H2O2 which can easily diffuse to the extramitochondrial space. Whereas ebselen required the presence of reduced glutathione as a reductant to grant its protective effect, TSA was fully reduced by mitochondrial components. Decrease in the oxygen concentration of the reaction medium also inhibits mitochondrial permeabilization and membrane protein thiol oxidation, in a concentration-dependent manner. The results presented in this report confirm that mitochondrial permeability transition induced by Ca2+ and inorganic phosphate is reactive oxygen species- dependent. The possible importance of TSA as an intracellular antioxidant, avoiding the onset of mitochondrial permeability transition, is discussed in the text.273211276612769Gunter, T.E., Gunter, K.K., Sheu, S.-S., Gavin, C.E., (1994) Am. J. Physiol., 267, pp. C313-C339Zoratti, M., Szabó, I., (1995) Biochim. Blophys. Acta, 1241, pp. 139-176Lehninger, A.L., Vercesi, A.E., Bababunmi, E.A., (1978) Proc. Natl. Acad. Sci. U. S. A., 79, pp. 6842-6846Vercesi, A.E., Kowaltowski, A.J., Grijalba, M.T., Meinicke, A.R., Castilho, R.F., (1997) Biosci. Rep., 17, pp. 43-52Castilho, R.F., Kowaltowski, A.J., Meinicke, A.R., Vercesi, A.E., (1995) Free Radical Biol. & Med., 18, pp. 479-486Kowaltowski, A.J., Castilho, R.F., Vercesi, A.E., (1995) Am. J. Physiol., 269, pp. C141-C147Valle, V.G.R., Fagian, M.M., Parentoni, L.S., Meinicke, A.R., Vercesi, A.E., (1993) Arch. Biockem. Biophys., 307, pp. 1-7Kowaltowski, A.J., Castilho, R.F., Vercesi, A.E., (1996) FEBS Lett., 378, pp. 150-152Kowaltowski, A.J., Castilho, R.F., Grijalba, M.T., Bechara, E.J.H., Vercesi, A.E., (1996) J. Biol. Chem., 271, pp. 2929-2934Fagian, M.M., Pereira-da-Silva, L., Martins, I.S., Vercesi, A.E., (1990) J. Biol. Chem., 265, pp. 19955-19960Castilho, R.F., Kowaltowski, A.J., Vercesi, A.E., (1996) J. Bioenerg. Biomembr., 28, pp. 523-529Scorrano, L., Petronilli, V., Bernardi, P., (1997) J. Biol. Chem., 272, pp. 12295-12299Pastorino, J.G., Snyder, J.W., Serroni, A., Hoek, J.B., Farber, J.L., (1993) J. Biol. Chem., 268, pp. 13791-13798Griffiths, E., Halestrap, A.P., (1995) Biochem. J., 307, pp. 93-98Zamzami, N., Hirsch, T., Dallaporta, B., Petit, P.X., Kroemer, G., (1997) J. Bioenerg. Biomembr., 29, pp. 185-193Skulachev, V.P., (1996) FEBS Lett., 397, pp. 7-10Kim, K., Kim, I.H., Lee, K.-Y., Rhee, S.G., Stadtman, E.R., (1988) J. Biol. Chem., 263, pp. 4704-4711Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G., Rhee, S.G., (1994) Proc. Natl. Acad. Sci. U. S. A., 91, pp. 7017-7021Chae, H.Z., Chung, S.J., Rhee, S.G., (1994) J. Biol. Chem., 269, pp. 27670-27678Netto, L.E.S., Chae, H.Z., Kang, S.-W., Rhee, S.G., Stadtman, E.R., (1996) J. Biol. Chem., 271, pp. 15315-15321Nogoceke, E., Gommel, D.U., Kieb, M., Kalisz, H.M., Flohé, L., (1997) Biol. Chem., 378, pp. 827-836Kim, I.H., Kim, K., Rhee, S.G., (1989) Proc. Natl. Acad. Sci. U. S. A., 86, pp. 6018-6022Watabe, S., Kohno, H., Kouyama, H., Hiroi, T., Yago, N., Nakazawa, T., (1994) J. Biochem. (Tokyo), 115, pp. 648-654Ishii, T., Kawane, T., Taketani, S., Bannai, S., (1995) Biochem. Biophys. Res. Commun., 216, pp. 970-975Sies, H., (1993) Free Radical Biol. & Med., 14, pp. 313-323Kowaltowski, A.J., Vercesi, A.E., Castilho, R.F., (1997) Biochim. Biophys. Acta, 1318, pp. 385-402Boveris, A., Martino, E., Stoppani, A.O.M., (1977) Anal. Biochem., 80, pp. 145-158Chae, H.Z., Uhm, T.B., Rhee, S.G., (1994) Proc. Natl. Acad. Sci. U. S. A., 91, pp. 7022-7026Tsuji, K., Copeland, N.G., Jenkins, N.A., Obinata, M., (1995) Biochem. J., 307, pp. 377-381Zhang, P., Liu, B., Kang, S.W., Seo, M.S., Rhee, S.G., Obeid, L.M., (1997) J. Biol. Chem., 272, pp. 30615-3061
Expression Of A Thioredoxin Peroxidase In Insulin-producing Cells
No full textThe presence of thioredoxin peroxidase (TPx), also known as thiol specific antioxidant (TSA), was investigated in neonatal and adult rat islets, and in the β-cell line HIT-T15. Western blotting of extracts from neonatal and adult pancreatic islets and from the tumoral cell line HIT-T15 revealed the presence of a 25 kDa protein that comigrated with purified yeast TPx. Endocrine pancreatic TPx accounted for approximately 0.01% of the total protein content. Treatment with H 2O 2 for 3 h increased the expression of TPx in HIT-T15 cells. The distribution of TPx throughout the islet cells was confirmed by immunocytochemistry. Since pancreatic β-cells possess a weak antioxidant enzyme defense system, especially with regard to hydrogen peroxidase-decomposing enzymes, the presence of a TPx analog in islets suggests that this enzyme may play a role in protecting pancreatic cells against reactive oxygen species.286 II3S253S28Malaisse, W.J., Malaisse-Lagae, F., Sener, A., Determinants of the selective toxicity of alloxan to the pancreatic β-cell (1982) Proc Natl Acad Sci USA, 79, pp. 927-930Tiedge, M., Lortz, S., Drinkgem, J., Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin producing cells (1997) Diabetes, 46, pp. 1733-1742Eizirik, D.L., Flodstrom, M., Karlsen, A.E., The harmony of the spheres: Inducible nitric oxide synthase and related genes in pancreatic beta cells (1996) Diabetologia, 39, pp. 875-890Kim, K., Kim, I.H., Lee, K.Y., The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O 2 mixed function oxidation system (1988) J Biol Chem, 263, pp. 4704-4710Kim, M., Kim, K., Rhee, S.G., Induction of an antioxidant protein of Saccharomyces cerevisiae by O 2, Fe 3-, or 2-mecaptoethanol (1989) Proc Natl Acad Sci USA, 86, pp. 6018-6022Netto, L.E.S., Chae, H.Z., Kang, S.W., Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties (1996) J Biol Chem, 271, pp. 15315-15321Zhang, P., Liu, B., Kang, S.W., Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2 (1997) J Biol Chem, 272, pp. 30615-30618Hotta, M., Tashiro, F., Ikegami, H., Pancreatic beta cell-specific expression of thioredoxin, an antioxidative and antiapoptotic protein, prevents autoimmune and streptozotocin-induced diabetes (1998) J Expl Med, 188, pp. 1445-1451Chae, H.Z., Uhm, T.B., Rhee, S.G., Dimerization of thiol-specific antioxidant and the essential role of cysteine 47 (1994) Proc Natl Acad Sci USA, 91, pp. 7022-7026Chen, H., Carlson, E.C., Pellet, L., Overexpression of metallothionein in pancreatic beta-cells reduces streptozotocin-induced DNA damage and diabetes (2001) Diabetes, 50, pp. 2040-204
Redox Regulation Of The Proteasome Via S-glutathionylation
No full textThe proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis. The central catalytic complex of the proteasome is called the 20S core particle. The majority of these are flanked on one or both sides by regulatory units. Most common among these units is the 19S regulatory unit. When coupled to the 19S unit, the complex is termed the asymmetric or symmetric 26S proteasome depending on whether one or both sides are coupled to the 19S unit, respectively. The 26S proteasome recognizes poly-ubiquitinylated substrates targeted for proteolysis. Targeted proteins interact with the 19S unit where they are deubiquitinylated, unfolded, and translocated to the 20S catalytic chamber for degradation. The 26S proteasome is responsible for the degradation of major proteins involved in the regulation of the cellular cycle, antigen presentation and control of protein synthesis. Alternatively, the proteasome is also active when dissociated from regulatory units. This free pool of 20S proteasome is described in yeast to mammalian cells. The free 20S proteasome degrades proteins by a process independent of poly-ubiquitinylation and ATP consumption. Oxidatively modified proteins and other substrates are degraded in this manner. The 20S proteasome comprises two central heptamers (β-rings) where the catalytic sites are located and two external heptamers (α-rings) that are responsible for proteasomal gating. Because the 20S proteasome lacks regulatory units, it is unclear what mechanisms regulate the gating of α-rings between open and closed forms. 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Functional and evolutionary characterization of Ohr proteins in eukaryotes reveals many active homologs among pathogenic fungi
No full textOhr and OsmC proteins comprise two subfamilies within a large group of proteins that display Cys-based, thiol dependent peroxidase activity. These proteins were previously thought to be restricted to prokaryotes, but we show here, using iterated sequence searches, that Ohr/OsmC homologs are also present in 217 species of eukaryotes with a massive presence in Fungi (186 species). Many of these eukaryotic Ohr proteins possess an N-terminal extension that is predicted to target them to mitochondria. We obtained recombinant proteins for four eukaryotic members of the Ohr/OsmC family and three of them displayed lipoyl peroxidase activity. Further functional and biochemical characterization of the Ohr homologs from the ascomycete fungus Mycosphaerella fijiensis Mf_1 (MfOhr), the causative agent of Black Sigatoka disease in banana plants, was pursued. Similarly to what has been observed for the bacterial proteins, we found that: (i) the peroxidase activity of MfOhr was supported by DTT or dihydrolipoamide (dithiols), but not by β-mercaptoethanol or GSH (monothiols), even in large excess; (ii) MfOhr displayed preference for organic hydroperoxides (CuOOH and tBOOH) over hydrogen peroxide; (iii) MfOhr presented extraordinary reactivity towards linoleic acid hydroperoxides (k=3.18 (±2.13)×108 M−1 s−1). Both Cys87 and Cys154 were essential to the peroxidase activity, since single mutants for each Cys residue presented no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides. The pKa value of the Cysp residue was determined as 5.7±0.1 by a monobromobimane alkylation method. Therefore, eukaryotic Ohr peroxidases share several biochemical features with prokaryotic orthologues and are preferentially located in mitochondria. Keywords: Ohr/OsmC, Thiol-dependent peroxidases, Phylogen
Measuring the effect of customer relationship management (CRM) components on the non financial performance of commercial banks: Egypt case
No full textThis paper presents customer relationship management (CRM) components as applied on the Egyptian Commercial Banks, examined from the bankers' point of view. Then, it intends to measure their effect on the level of customer satisfaction and loyalty from the customers’ point of view as examples of the non financial performance measures. The paper is quantitative in nature and consists of two different structured questionnaires using convenience/quota sampling. The first involved 180 employees in order to measure CRM applicability, and the second involved 270 customers to measure the level of customer satisfaction and loyalty and their effect on the Egyptian Commercial Banks' financial performance The findings show that the selected banks apply CRM components but the level of application differs from one bank to another. The results showed a significant positive relationship between CRM and customer satisfaction in the Egyptian Commercial Banks, when applying them together and not separately. In addition, there is a strong positive effect between customer satisfaction and loyalty which was reflected on the Commercial Banks' financial performance. The findings confirm the importance of studying and implementing CRM to achieve customer loyalty and improve the Egyptian Commercial Banks financial performance. Banks wishing to improve their relationships with customers need to focus on the CRM components to develop relevant and effective marketing strategies and tactics. The paper measures the CRM as a multidimensional construct as applied on the Egyptian Commercial Banks and relate it to the achievement of the ultimate goal of retaining customers to gaining a sustainable competitive advantage and achieve more profits
Gestão da drenagem urbana na bacia hidrográfica do rio Itajaí-Açu
No full textA urbanização, se não planejada, traz diversos impactos à sociedade e ao meio ambiente. O aumento do escoamento superficial contribui na ocorrência de enchentes. A relação com o meio social contribui na ocorrência de desastres. Neste quesito, o Estado de Santa Catarina é frequentemente atingido por eventos chuvosos intensos, que causam inundações em todo território. A bacia hidrográfica do Rio Itajaí-Açu se sobressai, em Santa Catarina, como a mais afetada por desastres relacionados a inundações, com 480 registros em um período de 21 anos. As constantes inundações na bacia demonstram a pouca atenção dedicada à área de drenagem. Desta forma o presente trabalho avaliou a gestão desta componente, integrado com a gestão do saneamento. O principal método utilizado foi à aplicação de questionários nos municípios que possuem sede dentro da bacia. Verificou-se que o abastecimento de água é o item que possui maior cobertura, enquanto a coleta do esgotamento sanitário ainda está em fase de desenvolvimento. Apesar da maioria dos municípios da bacia afirmar possuir sistema de drenagem, verificou-se que não há uma gestão eficiente nem responsáveis qualificados. Este motivo, aliado ao gerenciamento atual, pode contribuir para o incremento das inundações e alagamentos na bacia hidrográfica do Rio Itajaí-Açu
Ca2+-induced Increased Lipid Packing And Domain Formation In Submitochondrial Particles. A Possible Early Step In The Mechanism Of Ca2+- Stimulated Generation Of Reactive Oxygen Species By The Respiratory Chain
No full textCa2+ and P(i) accumulation by mitochondria triggers a number of alterations leading to nonspecific increase in inner membrane permeability [Kowaltowski, A. J., et al. (1996) J. Biol. Chem. 271, 29292934]. The molecular nature of the membrane perturbation that precedes oxidative damage is still unknown. EPR spectra of spin probes incorporated in submitochondrial particles (SMP) and in model membranes suggest that Ca2+-cardiolipin (CL) complexation plays an important role. Ca2+-induced lipid domain formation was detected in SMP but not in mitoplasts, in SMP extracted lipids, or in CL- containing liposomes. The results were interpreted in terms of Ca2+ sequestration of CL tightly bound to membrane proteins, in particular the ADP-ATP carrier, and formation of CL-enriched strongly immobilized clusters in lipid shells next to boundary lipid. The in-plane lipid and protein rearrangement is suggested to cause increased reactive oxygen species production in succinate-supplemented, antimycin A-poisoned SMP, favoring the formation of carbon-centered radicals, detected by EPR spin trapping. Removal of tightly bound CL is also proposed to cause protein aggregation, facilitating intermolecular thiol oxidation. Lipid peroxidation was also monitored by the disappearance of the nitroxide EPR spectrum. The decay was faster for nitroxides in a more hydrophobic environment, and was inhibited by butylated hydroxytoluene, by EGTA, or by substituting Mg2+ for Ca2+. In addition, Ca2+ caused an increase in permeability, evidenced by the release of carboxyfluorescein from respiring SMP. The results strongly support Ca2+ binding to CL as one of the early steps in the molecular mechanism of Ca2+- induced nonspecific inner mitochondrial membrane permeabilization.38401327913287Zoratti, M., Szabò, I., (1995) Biochim. Biophys. 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Behind the medical mask : medical technology and medical power
No full textThis thesis explores the role of technology as a resource in the
structure of medical domination of birth and death, stressing
technology's pivotal position at the intersection of control and
uncertainty.
Based in Intensive Care and Obstetrics (between which the health status
of patients diverges sharply), it notes the convergence of technology
used and examines the contest for control within the labour process.
This includes using technology to facilitate a 'standardized' birth or
death; a more retrospectively defensible event. In general, the
'burden of proof' is concluded to lie with those wishing not to
intervene rather than the reverse.
Given the (cognitively male) biomedical model, mind-body dualism is an
assumption embedded in medical technology: this is especially
significant in childbirth, where it fractures the woman's ontological
experience of giving birth. Its positivistic and pathological
emphasis is associated with a reification of processes and a
commodification of their 'solution': which becomes located in
technology. It is argued that commodification in health provision will
increase with the further application of market principles to the NHS.
It is concluded that 'uncertainty', endemic to medicine and a possible
challenge to control, is proactively manipulated and pressed into the
service of medical domination. Technology is used to mask uncertainty
and aid the medical profession's control of patients/relatives, and
subordinate work groups.
A technological fix may be viewed as the opposite to re-discovering
societal dreams and myths, however, more paradoxically, it is concluded
that dreams and myths have become attached to technology. Thus, the
symbolic role of technology is: to provide hope of continued survival
(or cure), the veiling of existential uncertainty and the offer of
'absolution' - should all efforts fail (a freedom from guilt in the
assurance that "everything possible was tried"). Its 'heroic' project
is viewed as an existentially 'masculine' health provision and
'feminized' health care is posited as an alternative
Mitochondria And Reactive Oxygen Species
No full textMitochondria are a quantitatively relevant source of reactive oxygen species (ROS) in the majority of cell types. Here we review the sources and metabolism of ROS in this organelle, including the conditions that regulate the production of these species, such as mild uncoupling, oxygen tension, respiratory inhibition, Ca2+ and K+ transport, and mitochondrial content and morphology. We discuss substrate-, tissue-, and organism-specific characteristics of mitochondrial oxidant generation. Several aspects of the physiological and pathological roles of mitochondrial ROS production are also addressed. © 2009 Elsevier Inc. All rights reserved.474333343Hinkle, P.C., Butow, R.A., Racker, E., Chance, B., Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles (1967) J. Biol. 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