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Cited by 222Metalloenzymes and iron-sulfur proteinsAnaerobic Digestion and Biogas ProductionEnzyme Structure and Function

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Energy-Converting [NiFe] Hydrogenases from Archaea and Extremophiles: Ancestors of Complex I

Hedderich, Reiner·2004·Journal of Bioenergetics and Biomembranes
DOI 10.1023/b:jobb.0000019599.43969.33
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Abstract

[NiFe] hydrogenases are well-characterized enzymes that have a key function in the H2 metabolism of various microorganisms. In the recent years a subfamily of [NiFe] hydrogenases with unique properties has been identified. The members of this family form multisubunit membrane-bound enzyme complexes composed of at least four hydrophilic and two integral membrane proteins. These six conserved subunits, which built the core of these hydrogenases, have closely related counterparts in energy-conserving NADH:quinone oxidoreductases (complex I). However, the reaction catalyzed by these hydrogenases differs significantly from the reaction catalyzed by complex I. For some of these hydrogenases the physiological role is to catalyze the reduction of H+ with electrons derived from reduced ferredoxins or poly-ferredoxins. This exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation. Other members of this hydrogenase family mainly function to provide the cell with reduced ferredoxin with H2 as electron donor in a reaction driven by reverse electron transport. As complex I these hydrogenases function as ion pumps and have therefore been designated as energy-converting [NiFe] hydrogenases.

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  1. Albracht, S. P., and Hedderich, R. (2000). FEBS Lett. 485, 1-6. · DOI
  2. Albracht, S. P. J. (1994). Biochim. Biophys. Acta 1188, 167-204. · DOI
  3. Andrews, S. C., Berks, B. C., McClay, J., Ambler, A., Quail, M. A., Golby, P., and Guest, J. R. (1997). Microbiology 143, 3633-3647. · DOI
  4. Bao, Q., Tian, Y., Li, W., Xu, Z., Xuan, Z., Hu, S., Dong, W., Yang, J., Chen, Y., Xue, Y., Xu, Y., Lai, X., Huang, L., Dong, X., Ma, Y., Ling, L., Tan, H., Chen, R., Wang, J., Yu, J., and Yang, H. (2002). Genome Res. 12, 689-700. f · DOI
  5. Bertram, P. A., and Thauer, R. K. (1994). Eur. J. Biochem. 226, 811-818. · DOI
  6. Blokesch, M., Paschos, A., Theodoratou, E., Bauer, A., Hube, M., Huth, S., and Bock, A. (2002). Biochem. Soc. Trans. 30, 674-680. · DOI
  7. Bock, A. K., Kunow, J., Glasemacher, J., and Schönheit, P. (1996). Eur. J. Biochem. 237, 35-44. · DOI
  8. Böhm, R., Sauter, M., and Böck, A. (1990). Mol. Microbiol. 4, 231-243. · DOI
  9. Bonam, D., and Ludden, P. W. (1987). J. Biol. Chem. 262, 2980-2987. · DOI
  10. Bott, M., Eikmanns, B., and Thauer, R. K. (1986). Eur. J. Biochem. 159, 393-398. · DOI
  11. Bott, M., and Thauer, R. K. (1989). Eur. J. Biochem. 179, 469-472. · DOI
  12. Brandt, U., Kerscher, S., Drose, S., Zwicker, K., and Zickermann, V. (2003). FEBS Lett. 545, 9-17. · DOI
  13. Bult, C. J., White, O., Olsen, G. J., Zhou, L., Fleischmann, R. D., Sutton, G. G., Blake, J. A., FitzGerald, L. M., Clayton, R. A., Gocayne, J. D., Kerlavage, A. R., Dougherty, B. A., Tomb, J. F., Adams, M. D., Reich, C. I., Overbeek, R., Kirkness, E. F., Weinstock, K. G., Merrick, J. M., Glodek, A., Scott, J. L., Geoghagen, N. S. M., and Venter, J. C. (1996). Science 273, 1058-1073. · DOI
  14. Darrouzet, E., Issartel, J. P., Lunardi, J., and Dupuis, A. (1998). FEBS Lett. 431, 34-38. · DOI · Paper page
  15. Deppenmeier, U., Müller, V., and Gottschalk, G. (1996). Arch. Microbiol. 165, 149-163. · DOI
  16. Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R., and Meyer, O. (2001). Science 293, 1281-1285. · DOI
  17. Drennan, C. L., Heo, J., Sintchak, M. D., Schreiter, E., and Ludden, P. W. (2001). Proc. Natl. Acad. Sci. U.S.A. 98, 11973-11978. · DOI
  18. Ensign, S. A., and Ludden, P. W. (1991). J. Biol. Chem. 266, 18395-18403. · DOI
  19. Ferry, J. G. (1997). Biofactors 6, 25-35. · DOI
  20. Fox, J. D., He, Y., Shelver, D., Roberts, G. P., and Ludden, P. W. (1996b). J. Bacteriol. 178, 6200-6208. · DOI
  21. Fox, J. D., Kerby, R. L., Roberts, G. P., and Ludden, P. W. (1996a). J. Bacteriol. 178, 1515-1524. · DOI
  22. Friedrich, T., and Scheide, D. (2000). FEBS Lett. 479, 1-5. · DOI
  23. Friedrich, T., and Weiss, H. (1997). J. Theor. Biol. 187, 529-540. · DOI
  24. Garcin, E., Montet, Y., Volbeda, A., Hatchikian, C., Frey, M., and Fontecilla-Camps, J. C. (1998). Biochem. Soc. Trans. 26, 396-401. · DOI
  25. Hamamoto, T., Hashimoto, M., Hino, M., Kitada, M., Seto, Y., Kudo, T., and Horikoshi, K. (1994). Mol. Microbiol. 14, 939-946. · DOI
  26. Ingledew, W. J., and Ohnishi, T. (1980). Biochem. J. 186, 111-117. · DOI
  27. Kaesler, B., and Schönheit, P. (1989a). Eur. J. Biochem. 184, 223-232. · DOI
  28. Kaesler, B., and Schönheit, P. (1989b). Eur. J. Biochem. 186, 309-316. · DOI
  29. Kashani-Poor, N., Zwicker, K., Kerscher, S., and Brandt, U. (2001). J. Biol. Chem. 276, 24082-24087. · DOI
  30. Kerby, R. L., Hong, S. S., Ensign, S. A., Coppoc, L. J., Ludden, P. W., and Roberts, G. P. (1992). J. Bacteriol. 174, 5284-5294. · DOI
  31. Kerby, R. L., Ludden, P. W., and Roberts, G. P. (1995). J. Bacteriol. 177, 2241-2244. · DOI
  32. Kerby, R. L., Ludden, P. W., and Roberts, G. P. (1997). J. Bacteriol. 179, 2259-2266. · DOI
  33. Künkel, A., Vorholt, J. A., Thauer, R. K., and Hedderich, R. (1998). Eur. J. Biochem. 252, 467-476. · DOI
  34. Kurkin, S., Meuer, J., Koch, J., Hedderich, R., and Albracht, S. P. (2002). Eur. J. Biochem. 269, 6101-6111. · DOI
  35. Malki, S., Saimmaime, I., De Luca, G., Rousset, M., Dermoun, Z., and Belaich, J. P. (1995). J. Bacteriol. 177, 2628-2636. · DOI
  36. Meuer, J., Bartoschek, S., Koch, J., Künkel, A., and Hedderich, R. (1999). Eur. J. Biochem. 265, 325-335. · DOI
  37. Meuer, J., Kuettner, H. C., Zhang, J. K., Hedderich, R., and Metcalf, W. W. (2002). Proc. Natl. Acad. Sci. U.S.A. 99, 5632-5637. · DOI
  38. Nicolet, Y., Cavazza, C., and Fontecilla-Camps, J. C. (2002). J. Inorg. Biochem. 91, 1-8. · DOI
  39. Putnoky, P., Kereszt, A., Nakamura, T., Endre, G., Grosskopf, E., Kiss, P., and Kondorosi, A. (1998). Mol. Microbiol. 28, 1091-1101. · DOI
  40. Sapra, R., Bagramyan, K., and Adams, M. W. (2003). Proc. Natl. Acad. Sci. U.S.A. 100, 7545-7550. · DOI
  41. Sapra, R., Verhagen, M., and Adams, M. W. W. (2000). J. Bacteriol. 182, 3423-3428. · DOI
  42. Sauter, M., Böhm, R., and Böck, A. (1992). Mol. Microbiol. 6, 1523-1532. · DOI
  43. Schwarz, E., and Friedrich, B. (2003). In The Prokaryotes: An Evolving Electronic Resource for the Microbiological Community (Dworkin, M., ed.), Springer, New York. Retrieved from http://141.150.157.117:8080/prokPUB/index.htm
  44. Shelver, D., Kerby, R. L., He, Y., and Roberts, G. P. (1997). Proc. Natl. Acad. Sci. U.S.A. 94, 11216-11220. · DOI · Paper page
  45. Silva, P. J., van den Ban, E. C., Wassink, H., Haaker, H., de Castro, B., Robb, F. T., and Hagen, W. R. (2000). Eur. J. Biochem. 267, 6541-6551. · DOI
  46. Skibinski, D. A., Golby, P., Chang, Y. S., Sargent, F., Hoffman, R., Harper, R., Guest, J. R., Attwood, M. M., Berks, B. C., and Andrews, S. C. (2002). J. Bacteriol. 184, 6642-6653. · DOI
  47. Slesarev, A. I., Mezhevaya, K. V., Makarova, K. S., Polushin, N. N., Shcherbinina, O. V., Shakhova, V. V., Belova, G. I., Aravind, L., Natale, D. A., Rogozin, I. B., Tatusov, R. L., Wolf, Y. I., Stetter, K. O., Malykh, A. G., Koonin, E. V., and Kozyavkin, S. A. (2002). Proc. Natl. Acad. Sci. U.S.A. 99, 4644-4649. · DOI
  48. Soboh, B., Linder, D., and Hedderich, R. (2002). Eur. J. Biochem. 269, 5712-5721. · DOI
  49. Svetlichny, V. A., Sokolova, T. G., Gerhardt, M., Ringpfeil, M., Kostrikina, N. A., and Zavarzin, G. A. (1991). Syst. Appl. Microbiol. 14, 254-260. · DOI
  50. Svetlitchnyi, V., Peschel, C., Acker, G., and Meyer, O. (2001). J. Bacteriol. 183, 5134-5144. · DOI
  51. Tersteegen, A., and Hedderich, R. (1999). Eur. J. Biochem. 264, 930-943. · DOI
  52. Thauer, R. K. (1998). Microbiology 144, 2377-2406. · DOI
  53. Thauer, R. K., Klein, A. R., and Hartmann, G. C. (1996). Chem. Rev. 96, 3031-3042. · DOI
  54. Tran-Betcke, A., Warnecke, U., Bocker, C., Zaborosch, C., and Friedrich, B. (1990). J. Bacteriol. 172, 2920-2929. · DOI
  55. Uffen, R. L. (1976). Proc. Natl. Acad. Sci. U.S.A. 73, 3298-3302. · DOI
  56. Vignais, P. M., Billoud, B., and Meyer, J. (2001). FEMS Microbiol. Rev. 25, 455-501. · DOI
  57. Volbeda, A., Charon, M. H., Piras, C., Hatchikian, E. C., Frey, M., and Fontecilla-Camps, J. C. (1995). Nature 373, 580-587. · DOI
  58. Vorholt, J. A., Vaupel, M., and Thauer, R. K. (1996). Eur. J. Biochem. 236, 309-317. · DOI
  59. Winner, C., and Gottschalk, G. (1989). FEMS Microbiol. Lett. 65, 259-264.
  60. Xue, Y., Xu, Y., Liu, Y., Ma, Y., and Zhou, P. (2001). Int. J. Syst. Evol. Microbiol. 51, 1335-1341. · DOI
  61. Yagi, T., Yano, T., Di Bernardo, S., and Matsuno-Yagi, A. (1998). Biochim. Biophys. Acta 1364, 125-133. · DOI
  62. Yano, T., and Ohnishi, T. (2001). J. Bioenerg. Biomembr. 33, 213-222. · DOI

Metadata

Authors
Hedderich, R.
Affiliations
Max Planck Institute for Terrestrial Microbiology (DE)
Corresponding author
Hedderich, Reiner
Venue
Journal of Bioenergetics and Biomembranes
Publisher
Springer Science and Business Media LLC
Published
2004-02
Volume
36
Issue
1
Pages
65-75
ISSN
  • 0145-479X (ISSN-L)
  • 1573-6881
DOI
10.1023/b:jobb.0000019599.43969.33
OpenAlex
W2085385457
Cited by
222
References
64
Citations by year
2026: 2 · 2025: 1 · 2024: 3 · 2023: 6 · 2022: 5 · 2021: 7 · 2020: 11 · 2019: 8 · 2018: 15 · 2017: 8 · 2016: 12 · 2015: 8 · 2014: 20 · 2013: 12 · 2012: 12
FWCI
2.75
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Journal of Bioenergetics and Biomembranes (publishedVersion)
  • PubMed (publishedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Anaerobic Digestion and Biogas Production
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
[NiFe] hydrogenase, archaea, extremophiles, electron transport phosphorylation, reverse electron transfer, ferredoxin reduction, ion pumps, hydrogen metabolism
MeSH terms
Archaea, Cell Membrane, Energy Transfer, Hydrogenase, Oxidation-Reduction, Halobacteriales, Conserved Sequence, Sequence Homology, Amino Acid, Evolution, Molecular, Electron Transport Complex I

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