NMR assignment of the apo-form of a Desulfovibrio gigas protein containing a novel Mo-Cu cluster,
Pauleta, Sofia R., Duarte Americo G., Carepo Marta S., Pereira Alice S., Tavares Pedro, Moura Isabel, and Moura Jose J. G.
, Biomolecular Nmr Assignments, Jul, Volume {1}, Number {1}, p.{81-83}, (2007)
AbstractWe report the 98% assignment of the apo-form of an orange protein, containing a novel Mo-Cu cluster isolated from Desulfovibrio gigas. This protein presents a region where backbone amide protons exchange fast with bulk solvent becoming undetectable. These residues were assigned using C-13-detection experiments.
A novel type of catalytic copper cluster in nitrous oxide reductase,
Brown, K., Tegoni M., Prudencio M., Pereira A. S., Besson S., Moura J. J., Moura I., and Cambillau C.
, Nature Structural Biology, Apr, Volume {7}, Number {3}, 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA, p.{191-195}, (2000)
AbstractNitrous oxide (N(2)O) is a greenhouse gas, the third most significant contributor to global warming. As a key process for N(2)O elimination from the biosphere, N(2)O reductases catalyze the two-electron reduction of N(2)O to N(2). These 2 x 65 kDa copper enzymes are thought to contain a CuA electron entry site, similar to that of cytochrome c oxidase, and a CuZ catalytic center. The copper anomalous signal was used to solve the crystal structure of N(2)O reductase from Pseudomonas nautica by multiwavelength anomalous dispersion, to a resolution of 2.4 Angstrom. The structure reveals that the CuZ center belongs to a new type of metal cluster, in which four copper ions are liganded by seven histidine residues. N(2)O binds to this center via a single copper ion. The remaining copper ions might act as an electron reservoir, assuring a fast electron transfer and avoiding the formation of dead-end products.