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Oxybenzone or benzophenone-3 or BP-3 (trade names Milestab 9, Eusolex 4360, Escalol 567, KAHSCREEN BZ-3) is an organic compound belonging to the class of aromatic ketones known as benzophenones. It takes the form of pale-yellow crystals that are readily soluble in most organic solvents.
An electron transport chain (ETC [1]) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H + ions) across a membrane.
MnhC - 113 and 3; MnhD - 498 and 13; MnhE - 159 and 4; MnhF - 97 and 3; MnhG - 118 and 3; In view of the complexity of the system, large variation in subunit structure, and the homology with NDH family protein constituents, a complicated energy coupling mechanism, possibly involving a redox reaction, cannot be ruled out.
Benzophenone is a naturally occurring organic compound with the formula (C 6 H 5) 2 CO, generally abbreviated Ph 2 CO. Benzophenone has been found in some fungi, fruits and plants, including grapes. [4] It is a white solid with a low melting point and rose-like odor [5] that is soluble in organic solvents. Benzophenone is the simplest ...
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system. [1] [2] [3] [4]P450 enzymes usually function as a terminal oxidase in multicomponent electron-transfer chains, called P450-containing monooxygenase systems, although self-sufficient, non-monooxygenase P450s have been also described.
Proteins of the Proton-dependent Oligopeptide Transporter (POT) Family (also called the PTR (peptide transport) family) are found in animals, plants, yeast, archaea and both Gram-negative and Gram-positive bacteria, and are part of the major facilitator superfamily. The transport of peptides into cells is a well-documented biological phenomenon ...
Schematic of reaction center in the membrane, with Cytochrome C at top Bacterial photosynthetic reaction center. The bacterial photosynthetic reaction center has been an important model to understand the structure and chemistry of the biological process of capturing light energy. In the 1960s, Roderick Clayton was the first to purify the ...
Microbial rhodopsins, also known as bacterial rhodopsins, are retinal-binding proteins that provide light-dependent ion transport and sensory functions in halophilic [2] [3] and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for retinal .