31. Zhang B, Hemann CF, Hille R (2010) Kinetic and spectroscopic studies of the [molybdenumcopper] CO dehydrogenase from Oligotropha carboxidovorans. J Biol Chem
285:12571–12578. doi:10.1074/jbc.M109.076851
32. Dobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O (2002) Catalysis at a dinuclear
CuSMo(==O)OH cluster in a CO dehydrogenase resolved at 1.1-angstrom resolution. Proc
Natl Acad Sci U S A 99:15971–15976. doi:10.1073/pnas.212640899
33. Hofmann M, Kassube JK, Graf T (2005) The mechanism of Mo-/Cu-dependent CO dehydrogenase. J Biol Inorg Chem 10:490–495. doi:10.1007/s00775-005-0661-5
34. Jeoung J-H, Dobbek H (2007) Carbon dioxide activation at the Ni, Fe-cluster of anaerobic
carbon monoxide dehydrogenase. Science 318:1461–1464. doi:10.1126/science.1148481
35. Russell WK, Lindahl PA (1998) CO/CO 2 potentiometric titrations of carbon monoxide
dehydrogenase from Clostridium thermoaceticum and the effect of CO 2 . Biochemistry
37:10016–10026. doi:10.1021/bi980149b
36. Majumdar A, Sarkar S (2011) Bioinorganic chemistry of molybdenum and tungsten
enzymes: a structural-functional modeling approach. Coord Chem Rev 255:1039–1054.
doi:10.1016/j.ccr.2010.11.027
37. Jormakka M, Tornroth S, Byrne B, Iwata S (2002) Molecular basis of proton motive force
generation: structure of formate dehydrogenase-N. Science 295:1863–1868. doi:10.1126/
science.1068186
38. George GN, Costa C, Moura JJG, Moura I (1999) Observation of ligand-based redox
chemistry at the active site of a molybdenum enzyme. J Am Chem Soc 121:2625–2626.
doi:10.1021/ja9841761
39. Rivas MG, Gonzalez PJ, Brondino CD, Moura JJG, Moura I (2007) EPR characterization of
the molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans
ATCC 27774 upon formate reduction. J Inorg Biochem 101:1617–1622. doi:10.1016/j.
jinorgbio.2007.04.011
40. Bevers LE, Hagedoorn PL, Hagen WR (2009) The bioinorganic chemistry of tungsten. Coord
Chem Rev 253:269–290. doi:10.1016/j.ccr.2008.01.017
41. Raaijmakers HCA, Romao MJ (2006) Formate-reduced E. coli formate dehydrogenase H: the
reinterpretation of the crystal structure suggests a new reaction mechanism. J Biol Inorg
Chem 11:849–854. doi:10.1007/s00775-006-0129-2
42. Cerqueira NMFSA, Fernandes PA, Gonzalez PJ, Moura JJG, Ramos MJ (2013) The sulfur
shift: an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase.
Inorg Chem 52:10766–10772. doi:10.1021/ic3028034
43. Axley MJ, Bock A, Stadtman TC (1991) Catalytic properties of an Escherichia coli formate
dehydrogenase mutant in which sulfur replaces selenium. Proc Natl Acad Sci U S A
88:8450–8454. doi:10.1073/pnas.88.19.8450
44. Mota CS, Rivas MG, Brondino CD, Moura I, Moura JJG, Gonzalez PJ, Cerqueira NMFSA
(2011) The mechanism of formate oxidation by metal-dependent formate dehydrogenases.
J Biol Inorg Chem 16:1255–1268. doi:10.1007/s00775-011-0813-8
45. Raaijmakers H, Macieira S, Dias JM, Teixeira S, Bursakov S, Huber R, Moura JJG, Moura I,
Romao MJ (2002) Gene sequence and the 1.8 angstrom crystal structure of the tungstencontaining formate dehydrogenase from Desulfovibrio gigas. Structure 10:1261–1272.
doi:10.1016/s0969-2126(02)00826-2
46. Jones AK, Sillery E, Albracht SPJ, Armstrong FA (2002) Direct comparison of the
electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chem Commun
8:866–867. doi:10.1039/b201337a
47. Madden C, Vaughn MD, Dı ´ez-Pe ´rez I, Brown KA, King PW, Gust D, Moore AL, Moore TA
(2012) Catalytic turnover of [FeFe]-hydrogenase based on single-molecule imaging. J Am
Chem Soc 134(3):1577–1582. doi:10.1021/ja207461t
48. Barton BE, Whaley CM, Rauchfuss TB, Gray DL (2009) Nickel-iron dithiolato hydrides
relevant to the [NiFe]-hydrogenase active site. J Am Chem Soc 131(20):6942–6943.
doi:10.1021/ja902570u
264
L. Gan et al.
285:12571–12578. doi:10.1074/jbc.M109.076851
32. Dobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O (2002) Catalysis at a dinuclear
CuSMo(==O)OH cluster in a CO dehydrogenase resolved at 1.1-angstrom resolution. Proc
Natl Acad Sci U S A 99:15971–15976. doi:10.1073/pnas.212640899
33. Hofmann M, Kassube JK, Graf T (2005) The mechanism of Mo-/Cu-dependent CO dehydrogenase. J Biol Inorg Chem 10:490–495. doi:10.1007/s00775-005-0661-5
34. Jeoung J-H, Dobbek H (2007) Carbon dioxide activation at the Ni, Fe-cluster of anaerobic
carbon monoxide dehydrogenase. Science 318:1461–1464. doi:10.1126/science.1148481
35. Russell WK, Lindahl PA (1998) CO/CO 2 potentiometric titrations of carbon monoxide
dehydrogenase from Clostridium thermoaceticum and the effect of CO 2 . Biochemistry
37:10016–10026. doi:10.1021/bi980149b
36. Majumdar A, Sarkar S (2011) Bioinorganic chemistry of molybdenum and tungsten
enzymes: a structural-functional modeling approach. Coord Chem Rev 255:1039–1054.
doi:10.1016/j.ccr.2010.11.027
37. Jormakka M, Tornroth S, Byrne B, Iwata S (2002) Molecular basis of proton motive force
generation: structure of formate dehydrogenase-N. Science 295:1863–1868. doi:10.1126/
science.1068186
38. George GN, Costa C, Moura JJG, Moura I (1999) Observation of ligand-based redox
chemistry at the active site of a molybdenum enzyme. J Am Chem Soc 121:2625–2626.
doi:10.1021/ja9841761
39. Rivas MG, Gonzalez PJ, Brondino CD, Moura JJG, Moura I (2007) EPR characterization of
the molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans
ATCC 27774 upon formate reduction. J Inorg Biochem 101:1617–1622. doi:10.1016/j.
jinorgbio.2007.04.011
40. Bevers LE, Hagedoorn PL, Hagen WR (2009) The bioinorganic chemistry of tungsten. Coord
Chem Rev 253:269–290. doi:10.1016/j.ccr.2008.01.017
41. Raaijmakers HCA, Romao MJ (2006) Formate-reduced E. coli formate dehydrogenase H: the
reinterpretation of the crystal structure suggests a new reaction mechanism. J Biol Inorg
Chem 11:849–854. doi:10.1007/s00775-006-0129-2
42. Cerqueira NMFSA, Fernandes PA, Gonzalez PJ, Moura JJG, Ramos MJ (2013) The sulfur
shift: an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase.
Inorg Chem 52:10766–10772. doi:10.1021/ic3028034
43. Axley MJ, Bock A, Stadtman TC (1991) Catalytic properties of an Escherichia coli formate
dehydrogenase mutant in which sulfur replaces selenium. Proc Natl Acad Sci U S A
88:8450–8454. doi:10.1073/pnas.88.19.8450
44. Mota CS, Rivas MG, Brondino CD, Moura I, Moura JJG, Gonzalez PJ, Cerqueira NMFSA
(2011) The mechanism of formate oxidation by metal-dependent formate dehydrogenases.
J Biol Inorg Chem 16:1255–1268. doi:10.1007/s00775-011-0813-8
45. Raaijmakers H, Macieira S, Dias JM, Teixeira S, Bursakov S, Huber R, Moura JJG, Moura I,
Romao MJ (2002) Gene sequence and the 1.8 angstrom crystal structure of the tungstencontaining formate dehydrogenase from Desulfovibrio gigas. Structure 10:1261–1272.
doi:10.1016/s0969-2126(02)00826-2
46. Jones AK, Sillery E, Albracht SPJ, Armstrong FA (2002) Direct comparison of the
electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chem Commun
8:866–867. doi:10.1039/b201337a
47. Madden C, Vaughn MD, Dı ´ez-Pe ´rez I, Brown KA, King PW, Gust D, Moore AL, Moore TA
(2012) Catalytic turnover of [FeFe]-hydrogenase based on single-molecule imaging. J Am
Chem Soc 134(3):1577–1582. doi:10.1021/ja207461t
48. Barton BE, Whaley CM, Rauchfuss TB, Gray DL (2009) Nickel-iron dithiolato hydrides
relevant to the [NiFe]-hydrogenase active site. J Am Chem Soc 131(20):6942–6943.
doi:10.1021/ja902570u
264
L. Gan et al.