Structural variability of the active site of Fe-only hydrogenase and its hydrogenated forms

Abstract

Density functional calculations show that the (cys-S)- (CO)(CN)FeS₂(µ-CO)Fe(CO)(CN) active site of the Fe-only hydrogenase from Clostridium pasteurianum is redox ambivalent and stereochemically flexible at the CO and S bridges, and at the Fe atoms, and with bound hydrogen: the fundamentals of probable mechanisms are revealed.

References

1. M. W. W. Adams, Biochim. Biophys. Acta, 1990, 1020, 115.
2. S. P. J. Albracht, Biochim. Biophys. Acta, 1994, 1118, 167.
3. M. Frey, Struct. Bonding, 1998, 90, 97.
4. M. W. W. Adams and E. I. Stiefel, Science, 1998, 282, 1842.
5. R. Cammack, Nature, 1999, 397, 214.
6. A. Volbeda, M.-H. Charon, C. Piras, E. C. Hatchikian, M. Frey and J. C. Fontecilla-amps, Nature, 1995, 373, 580.
7. J. C. Fontecilla-Camps, M. Frey, E. Garcin, C. Hatchikian, Y. Montet, C. Piras, X. Vernede and A. Volbeda, Biochimie, 1997, 79, 661.
8. Y. Higuchi, T. Yagi and N. Yasuoka, Structure, 1997, 5, 1671.
9. J. W. Peters, W. N. Lanzilotta, B. J. Lemon and L. C. Seefeldt, Science, 1998, 282, 1853.
10. E. Garcin, X. Vernede, E. C. Hatchikian, A. Volbeda, M. Frey and J. C. Fontecilla-Camps, Structure, 1999, 7, 557.
11. Y. Higuchi, H. Ogata, K. Miki, N. Yasuoka and T. Yagi, Structure, 1999, 7, 549.
12. Y. Nicolet, C. Piras, P. Legrand, C. E. Hatchikian and J. C. Fontecilla-Camps, Structure, 1999, 7, 13.
13. A. J. Pierek, M. Hulstein, W. Hagen and S. P. J. Albracht, Eur. J. Biochem., 1998, 258, 572.
14. I. Dance, unpublished results.
15. I. G. Dance, in Transition Metal Sulfur Chemistry: Biological and Industrial Significance, ed. E. I. Stiefel and K. Matsumoto, American Chemical Society, Washington DC, USA, 1996, pp. 135–152.
16. I. G. Dance, J. Biol. Inorg. Chem., 1996, 1, 581.
17. I. Dance, Chem. Commun., 1998, 523.
18. J. W. Peters, personal communication, 1999.