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Ionic liquids (ILs) have now been acknowledged as reaction media for biotransformations. The first three examples were reported in this field in 2000, and since then, numerous applications have been reported for biocatalytic reactions using ILs. Two topics using ILs for enzymatic reactions have been reviewed from the standpoint of biocatalyst mediating organic synthesis; the first is "Biocatalysis in Ionic Liquids" which includes various types of biocatalytic reactions in ILs (section 2): (1) recent examples of lipase-mediated reactions using ILs as reaction media for biodiesel oil production and for sugar ester production, (2) oxidase-catalyzed reactions in ILs, (3) laccase-catalyzed reactions, (4) peroxidase-catalyzed reactions, (4) cytochrome-mediated reactions, (5) microbe-mediated hydrations, (6) protease-catalyzed reactions, (8) whole cell mediated asymmetric reduction of ketones, (10) acylase-catalyzed reactions, (11) glycosylation or cellulase-mediated hydrolysis of polysaccharides, (12) hydroxynitrile lyase-catalyzed reaction, (13) fluorinase or haloalkane dehydrogenase-catalyzed reaction, (14) luciferase-catalyzed reactions, and (15) biocatalytic promiscuity of enzymatic reactions for organic synthesis using ILs. The second is "Enzymes Activated by Ionic Liquids for Organic Synthesis", particularly describing the finding story of activation of lipases by the coating with a PEG-substituted IL (section 3). The author's opinion toward "Future Perspectives of Using ILs for Enzymatic Reactions" has also been discussed in section 4. [ABSTRACT FROM AUTHOR]

The article focuses on a study related to cellular respiration and perspective of protein pumping in the same. Topics discussed include coupling mechanism of respiratory electron transfer to the synthesis of adenosine triphosphate from adenosine diphosphate, generation of electrochemical proton gradient through oxidoreduction reactions of the respiratory chain, and arrangement of cytochromes in photosynthetic reaction center.

The article focuses on the reaction mechanism of bovine heart Cytochrome c Oxidase (CcO). Topics covered include the purification and crystallization of bovine heart CcO, how CcO lowers molecular oxygen (O2) in a reaction that is linked with proton pumping, structure and content of the metal cofactors of bovine heart CcO, and the structure and content of lipids.

The article presents a study on metalloproteins with cytochrome, iron-sulfur and copper redox centers. It mentions the presence of the hemoprotein in the inner mitochondrial membrane of eukaryotic organisms as well as in Gram-positive and negative bacteria. An overview of the redox attributes of designed 6-coordinate heme proteins which imitate electron transfer (ET) cytochromes is also provided.

The article offers information on endocannabinoid oxygenation by cyclooxygenases, lipoxygenases, and cytochromes P450. It describes the oxegenation of endocannabinoids and related compounds by eicosanoid pathways enzymes. It also presents a cross-talk between the endocannabinoid and eicosanoid signalling pathways.

The article offers information about the evidences that prove Cytochromes c′ are biological models for the S = 3⁄2,5⁄2 spin-state admixture. The study aims to ascertain the presence of a quantum mechanical spin-admixture ground state in the Cytochromes c′ and to clarify the significance and possible involvement of Arg/Lys-ImH interactions in its physico-chemical characteristics as well as its other properties.

The article provides information on the nature and functions of cytochromes c. They have relatively high thermodynamic stability. It can bind one or several c-type hemes. It functions like an electron transfer protein due to it's involvement in aerobic and anaerobic respiration. Cytochrome c serves as the pathway of hydrogen peroxide scavenging in Eukaryota.

Focuses on the theoretical perspective on the structure and mechanism by cytochrome P450 enzymes. Description of cytochrome P450 enzymes; Advantage of the advances in density functional theory; Presentation of the coverage, sources of computational results, and models of the enzyme.

Studies the structure and chemistry of cytochrome P450. Emphasis on the role of cytochrome P450 in biology; Presence of the cytochrome P450 in all branches of the tree of life that catalogs the diversity of life forms; Discussion on the formation of the peroxol/hydroperoxo complex.

Examines the synthetic models for heme-copper oxidase or cytochrome c oxidase which is important in biological respiration and in the dioxygen activation chemistry. Comparison between the subunits I and II of the two major classes of the heme-copper oxidase superfamily; Identification of the physical properties of the dioxygen adducts of heme-copper model complexes; Analysis of the heme-copper enzyme carbon monoxide (CO) adducts and heme-copper CO complexes; Probe on the structural, spectroscopic and magnetization properties of the oxidized heme-copper models.

Compares the geometric and electronic structure of low-spin ferro- and ferrihemes as models of the bis-histidine-ligated electron-transferring cytochromes. Use of electron paramagnetic resonance spectroscopic data for cytochromes in identifying axial ligands and their orientations; Identification of the early complexes in iron tetraphenylporphyrinates such as the non-hindered and hindered bis-imidazole complexes of TPPFe(III) and enigmatic bis-imidazole complex of TPPFe(III) with large axial ligand plane dihedral angle; Analysis of the electrochemical data for the FeIII/FeII couple of synthetic heme complexes.

Examines the functional analogues of the heme proteins cytochrome c oxidase (CcO), myoglobin (Mb) and hemoglobin (Hb). Responsibility of Hb and Mb in transporting and storing oxygen in many aerobic organisms; Comparison between the molecular origin of carbon oxide and oxygen discrimination by Mb and Hb; Analysis of the electrostatic and H-bonding effects on heme's affinity for small molecules; Illustration of the function of CcO in coupling the oxidation of ferrocytochrome c or ubiquinol.