The Experts below are selected from a list of 68523 Experts worldwide ranked by ideXlab platform
Milena Vukotic - One of the best experts on this subject based on the ideXlab platform.
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rcf1 mediates Cytochrome Oxidase assembly and respirasome formation revealing heterogeneity of the enzyme complex
Cell Metabolism, 2012Co-Authors: Milena Vukotic, Silke Oeljeklaus, Sebastian Wiese, Nora F Vogtle, Chris Meisinger, Helmut E Meyer, Anke Zieseniss, D M Katschinski, Daniel C JansAbstract:The terminal enzyme of the mitochondrial respiratory chain, Cytochrome Oxidase, transfers electrons to molecular oxygen, generating water. Within the inner mitochondrial membrane, Cytochrome Oxidase assembles into supercomplexes, together with other respiratory chain complexes, forming so-called respirasomes. Little is known about how these higher oligomeric structures are attained. Here we report on Rcf1 and Rcf2 as Cytochrome Oxidase subunits in S. cerevisiae. While Rcf2 is specific to yeast, Rcf1 is a conserved subunit with two human orthologs, RCF1a and RCF1b. Rcf1 is required for growth in hypoxia and complex assembly of subunits Cox13 and Rcf2, as well as for the oligomerization of a subclass of Cytochrome Oxidase complexes into respirasomes. Our analyses reveal that the Cytochrome Oxidase of mitochondria displays intrinsic heterogeneity with regard to its subunit composition and that distinct forms of respirasomes can be formed by complex variants.
Daniel C Jans - One of the best experts on this subject based on the ideXlab platform.
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rcf1 mediates Cytochrome Oxidase assembly and respirasome formation revealing heterogeneity of the enzyme complex
Cell Metabolism, 2012Co-Authors: Milena Vukotic, Silke Oeljeklaus, Sebastian Wiese, Nora F Vogtle, Chris Meisinger, Helmut E Meyer, Anke Zieseniss, D M Katschinski, Daniel C JansAbstract:The terminal enzyme of the mitochondrial respiratory chain, Cytochrome Oxidase, transfers electrons to molecular oxygen, generating water. Within the inner mitochondrial membrane, Cytochrome Oxidase assembles into supercomplexes, together with other respiratory chain complexes, forming so-called respirasomes. Little is known about how these higher oligomeric structures are attained. Here we report on Rcf1 and Rcf2 as Cytochrome Oxidase subunits in S. cerevisiae. While Rcf2 is specific to yeast, Rcf1 is a conserved subunit with two human orthologs, RCF1a and RCF1b. Rcf1 is required for growth in hypoxia and complex assembly of subunits Cox13 and Rcf2, as well as for the oligomerization of a subclass of Cytochrome Oxidase complexes into respirasomes. Our analyses reveal that the Cytochrome Oxidase of mitochondria displays intrinsic heterogeneity with regard to its subunit composition and that distinct forms of respirasomes can be formed by complex variants.
Christopher R Hayworth - One of the best experts on this subject based on the ideXlab platform.
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in vivo low level light therapy increases Cytochrome Oxidase in skeletal muscle
Photochemistry and Photobiology, 2010Co-Authors: Christopher R Hayworth, Julio C Rojas, Eimeira Padilla, Genevieve M Holmes, Eva C Sheridan, Francisco GonzalezlimaAbstract:: Low-level light therapy (LLLT) increases survival of cultured cells, improves behavioral recovery from neurodegeneration and speeds wound healing. These beneficial effects are thought to be mediated by upregulation of mitochondrial proteins, especially the respiratory enzyme Cytochrome Oxidase. However, the effects of in vivo LLLT on Cytochrome Oxidase in intact skeletal muscle have not been previously investigated. We used a sensitive method for enzyme histochemistry of Cytochrome Oxidase to examine the rat temporalis muscle 24 h after in vivo LLLT. The findings showed for the first time that in vivo LLLT induced a dose- and fiber type-dependent increase in Cytochrome Oxidase in muscle fibers. LLLT was particularly effective at enhancing the aerobic capacity of intermediate and red fibers. The findings suggest that LLLT may enhance the oxidative energy metabolic capacity of different types of muscle fibers, and that LLLT may be used to enhance the aerobic potential of skeletal muscle.
Francisco Gonzalezlima - One of the best experts on this subject based on the ideXlab platform.
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in vivo low level light therapy increases Cytochrome Oxidase in skeletal muscle
Photochemistry and Photobiology, 2010Co-Authors: Christopher R Hayworth, Julio C Rojas, Eimeira Padilla, Genevieve M Holmes, Eva C Sheridan, Francisco GonzalezlimaAbstract:: Low-level light therapy (LLLT) increases survival of cultured cells, improves behavioral recovery from neurodegeneration and speeds wound healing. These beneficial effects are thought to be mediated by upregulation of mitochondrial proteins, especially the respiratory enzyme Cytochrome Oxidase. However, the effects of in vivo LLLT on Cytochrome Oxidase in intact skeletal muscle have not been previously investigated. We used a sensitive method for enzyme histochemistry of Cytochrome Oxidase to examine the rat temporalis muscle 24 h after in vivo LLLT. The findings showed for the first time that in vivo LLLT induced a dose- and fiber type-dependent increase in Cytochrome Oxidase in muscle fibers. LLLT was particularly effective at enhancing the aerobic capacity of intermediate and red fibers. The findings suggest that LLLT may enhance the oxidative energy metabolic capacity of different types of muscle fibers, and that LLLT may be used to enhance the aerobic potential of skeletal muscle.
D M Katschinski - One of the best experts on this subject based on the ideXlab platform.
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rcf1 mediates Cytochrome Oxidase assembly and respirasome formation revealing heterogeneity of the enzyme complex
Cell Metabolism, 2012Co-Authors: Milena Vukotic, Silke Oeljeklaus, Sebastian Wiese, Nora F Vogtle, Chris Meisinger, Helmut E Meyer, Anke Zieseniss, D M Katschinski, Daniel C JansAbstract:The terminal enzyme of the mitochondrial respiratory chain, Cytochrome Oxidase, transfers electrons to molecular oxygen, generating water. Within the inner mitochondrial membrane, Cytochrome Oxidase assembles into supercomplexes, together with other respiratory chain complexes, forming so-called respirasomes. Little is known about how these higher oligomeric structures are attained. Here we report on Rcf1 and Rcf2 as Cytochrome Oxidase subunits in S. cerevisiae. While Rcf2 is specific to yeast, Rcf1 is a conserved subunit with two human orthologs, RCF1a and RCF1b. Rcf1 is required for growth in hypoxia and complex assembly of subunits Cox13 and Rcf2, as well as for the oligomerization of a subclass of Cytochrome Oxidase complexes into respirasomes. Our analyses reveal that the Cytochrome Oxidase of mitochondria displays intrinsic heterogeneity with regard to its subunit composition and that distinct forms of respirasomes can be formed by complex variants.
