Search

Methyl-coenzyme M reductase (MCR) catalyzes the methane-forming step in methanogenic archaea. The active enzyme harbors the nickel(I) hydrocorphin coenzyme F-430 as a prosthetic group and catalyzes the reversible reduction of methyl-coenzyme M (CH3-S-CoM) with coenzyme B (HS-CoM) to methane and CoM-S-S-CoB. MCR is also involved in anaerobic methane oxidation in reverse of methanogenesis and most probably in the anaerobic oxidation of ethane, propane, and butane. The challenging question is how the unreactive CH3-S thioether bond in methyl-coenzyme M and the even more unreactive C-H bond in methane and the other hydrocarbons are anaerobically cleaved. A key to the answer is the negative redox potential (Eo') of the Ni(II)F-430/Ni(I)F-430 couple below -600 mV and the radical nature of Ni(I)F-430. However, the negative one-electron redox potential is also the Achilles heel of MCR; it makes the nickel enzyme one of the most O2-sensitive enzymes known to date. Even under physiological conditions, the Ni(I) in MCR is oxidized to the Ni(II) or Ni(III) states, e.g., when in the cells the redox potential (E') of the CoM-S-S-CoB/HS-CoM and HS-CoB couple (Eo' = -140 mV) gets too high. Methanogens therefore harbor an enzyme system for the reactivation of inactivated MCR in an ATP-dependent reduction reaction. Purification of active MCR in the Ni(I) oxidation state is very challenging and has been achieved in only a few laboratories. This perspective reviews the function, structure, and properties of MCR, what is known and not known about the catalytic mechanism, how the inactive enzyme is reactivated, and what remains to be discovered.

5 Pags., The photoreaction center from the purple sulfur bacterium Ectothiorhodospira sp. was illuminated in the presence of reduced cytochrome c or dithionite under anaerobic conditions. This treatment first caused the monoelectronic reduction of both molecules of bacteriopheophytin (Bph), phi A and phi B, as witnessed by the appearance of EPR and optical signals typical of singly-reduced bacteriochlorins. Continued illumination under the same reducing conditions caused both of these signals to disappear. Such disappearance was accompanied by a complete bleaching of the Qx and Qy absorption bands of Bph but not of the corresponding transitions of bacteriochlorophyll (Bchl). These phenomena are interpreted by a double reduction of phi A and phi B. As long as the medium remained reducing and anaerobic, these changes were stable. Prolonged illumination under the same reducing conditions finally led to the bleaching of the Qx (600 nm) and Qy (800 nm) bands of Bchl but not of the 880-nm band. This generated no EPR or 645-nm absorption signals due to singly-reduced Bchl. The bleaching kinetics of the 800-nm band was biphasic and paralleled a shift of the peak wavelength. This is interpreted by a double reduction of both molecules of monomeric Bchl BA and BB in an undetermined order. After bleaching of the 800-nm band has reached saturation, the absorbance ratio of the 800/880-nm absorption bands remains constant, as would be expected if the ultimate spectrum was that of the primary electron donor. These experiments demonstrate the photoreduction of Bchl and allow the absorption spectrum of the primary donor to be measured for the first time.