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By Williams R.J.P.

Content material: organic nickel / J.C. Fontecilla-Camps -- Nickel in F₄₃₀ / J. Tesler -- Hemeproteins in anaerobes / I.A.C. Pereira, M. Teixeira, A.V. Xavier -- Evolutionary facets of copper binding facilities in copper proteins / B. Abolmaali, H.V. Taylor, U. Weser

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X-Ray Diffraction (Crystallographic) Studies . . . . . . . X-Ray A b s o r p t i o n (EXAFS) Studies ................... EPR Studies . . . . . . . . . . . . . . . . . Electrochemical Studies . . . . . . . . . . . . . Optical Spectroscopic Studies (UV-Vis, MCD) . . . . . . . Vibrational Spectroscopic Studies ( R a m a n ) . . . . . . . . 43 43 46 47 50 50 52 6 Theoretical Studies of F430 and Model Compounds (Molecular Mechanics) .

The reaction is catalyzed by methyl coenzyme M reductase, which is briefly described in Sect. 2. The concentration of CoM-S-S-HTP affects the first step of the methanogenic cycle, the formation of formyl-MFR [25]. The free thiol forms of CoM and HTP are then regenerated by a disulfide reductase [26]. -). This enzyme has been isolated from several organisms (including 36 J. Telser CO2H~ O N H H2N CO2H N H 2 C02H Methanofuran (MFR) OH O H H N ~ O H~O ~p/O A CO2H o -O- o j H Tetrahydromethanopterin(lq_4 MPT) OH OH 0 ~ O N p / O ~ N o.

Jannaschii and Mp. kandleri, are of particular interest as they are extreme hyperthermophiles (optimal growth at 85 ~ and 98~ respectively), thus representing organisms that appeared early in evolution. The ribosomal RNA ofMp. kandleri suggested that it was not closely relat- Nickel in F43o 37 ed to other methanogens [30]. Nevertheless, its MCR was quite similar to those of less thermophilic organisms. The complete genome of Mc. jannaschii has very recently been determined [31], which included identification of the genes coding for cofactor synthesis, MCR, and other methanogenic enzymes.

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