Catalytic Properties of Mitochondrial NADH-Ubiquinone Reductase (Complex I)

Biochemistry (Moscow)

Volumn 64, Issue 2, 1999, Pages 136-152

  Vinogradov, A D ^a   Gavrikova, E V ^a   Grivennikova, V G ^a   Zharova, T V ^a   Zakharova, N V ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Bovine heart mitochondria; Complex I; Enzyme hysteresis; NADH ubiquinone reductase; Respiratory chain

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

CATALYSIS; DRUG ANTAGONISM; ELECTRON TRANSPORT; ENZYMOLOGY; KINETICS; METABOLISM; MITOCHONDRION; REVIEW;

CATALYSIS; ELECTRON TRANSPORT; KINETICS; MITOCHONDRIA; NAD(P)H DEHYDROGENASE (QUINONE);

EID: 0033073095     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (160)

1. Singer, T. P., and Gutman, M. (1971) Adv. Enzymol., 34, 79-153.
2. Ragan, C. I. (1976) Biochim. Biophys. Acta, 456, 249-290.
3. Fearnley, I. M., and Walker, J. F. (1992) Biochim. Biophys. Acta, 1140, 105-134.
4. Weiss, H., Friedrich, T., Hofhaus, G., and Preis, D. (1991) Eur. J. Biochem., 197, 563-576.
5. Yagi, T. (1993) Biochim. Biophys. Acta, 1141, 1-17.
6. Rao, N. A., Felton, S. P., Huennekens, F. M., and Mackler, B. (1963) J. Biol. Chem., 238, 449-455.
7. Ohnishi, T. (1979) in Membrane Proteins in Energy Transduction (Capaldi, R. A., ed.) Dekker, New York, pp. 1-87.
8. Ohnishi, T., and Salerno, J. C. (1982) in Iron-Sulfur Proteins (Spiro, T., ed.) Vol. IV, Wiley Publishing Co. Inc., New York, pp. 285-327.
9. Beinert, H., and Albracht, S. P. J. (1982) Biochim. Biophys. Acta, 683, 245-277.
10. Sled, V. D., Friedrich, T., Leif, H., Weiss, H., Meinhardt, S. W., Fukumori, Y., Calhoun, M., Gennis, R. B., and Ohnishi, T. J. (1993) Bioenerg. Biomembr., 25, 347-356.
11. Vinogradov, A. D., Sled, V. D., Burbaev, D. Sh., Grivennikova, V. G., Moroz, I. A., and Ohnishi, T. (1995) FEBS Lett., 370, 83-87.
12. Berry, E. A., and Trumpower, B. L. (1985) in Coenzyme Q (Lenaz, G., ed.) John Wiley and Sons Ltd., New York, pp. 365-389.
13. Yu, C.-A., and Yu, L. J. (1993) Bioenerg. Biomembr., 25, 259-274.
14. Gennis, R., and Ferguson-Miller, S. (1995) Science, 269, 1063-1065.
15. Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinza-Itoh, K., Nakashima, R., Yano, R., and Yoshikawa, S. (1995) Science, 269, 1069-1074.
16. Brandt, U. (1997) Biochim. Biophys. Acta, 1318, 79-91.
17. Walker, J. E. (1992) Quart. Rev. Biophys., 25, 253-324.
18. Biochim. Biophys. Acta (Brandt, U., ed.) (1998) 1364.
19. Vinogradov, A. D. (1998) Biochim. Biophys. Acta, 1364, 169-185.
20. Hatefi, Y. (1978) Meth. Enzymol., 53, 3-4.
21. Singer, T. P., and Ramsay, R. R. (1992) in Molecular Mechanisms in Bioenergetics (Ernster, L., ed.) Elsevier Science Publishers B. V., Amsterdam, pp. 145-162.
22. Friedrich, T., Van Heek, P., Leif, H., Ohnishi, T., Forche, E., Kunze, B., Jansen, R., Trowitzsch-Keinast, W., Höfle, G., Reichenbach, H., and Weiss, H. (1994) Eur. J. Biochem., 219, 691-698.
23. Degli Esposti, M., Ghelli, A., Ratta, M., Cortes, D., and Estornell, E. (1994) Biochem. J., 301, 161-167.
24. Oettmeier, W., Masson, K., and Soll, M. (1992) Biochim. Biophys. Acta, 1099, 262-266.
25. Satoh, T., Miyoshi, H., Sakamoto, K., and Iwamura, H. (1996) Biochim. Biophys. Acta, 1273, 21-30.
26. Kean, E. A. (1970) Biochem. Pharmacol, 19, 2201-2210.
27. Kean, E. A., Gutman, M., and Singer, T. P. (1971) J. Biol. Chem., 246, 2346-2353.
28. Zharova, T. V., and Vinogradov, A. D. (1997) Biochim. Biophys. Acta, 1320, 256-264.
29. Kotlyar, A. B., and Vinogradov, A. D. (1990) Biochim. Biophys. Acta, 1019, 151-158.
30. King, T. E., Howard, R. L., Kettman, J., Hegdekar, B. M., Kuboyama, M., Mickel, K. S., and Possehl, E. A. (1966) in Flavins and Flavoproteins (Slater, E. C., ed.) Elsevier, Amsterdam, pp. 441-481.
31. Cremona, T., and Kearney, E. B. (1964) J. Biol. Chem., 239, 2328-2334.
32. King, T. E., and Howard, R. L. (1962) J. Biol. Chem., 237, 1686-1698.
33. Baugh, R. F., and King, T. E. (1972) Biochem. Biophys. Res. Commun., 49, 1165-1173.
34. Paech, C., Reynolds, J. G., Singer, T. P., and Holm, R. H. (1981) J. Biol. Chem., 256, 1922-1927.
35. Finel, M., Skehel, J. M., Albracht, S. P. J., Fearnley, I. M., and Walker, J. E. (1992) Biochemistry, 31, 11425- 11434.
36. Mackler, B. (1961) Biochim. Biophys. Acta, 50, 141-146.
37. Pharo, R. L., Sordahl, L. A., Vyas, S. R., and Sanadi, D. R. (1966) J. Biol. Chem., 241, 4771-4780.
38. Hatefi, Y., and Stempel, K. E. (1969) J. Biol. Chem., 244, 2350-2357.
39. Vinogradov, A. D. (1993) J. Bioenerg. Biomembr., 25, 367-375.
40. Sled, V. D., and Vinogradov, A. D. (1993) Biochim. Biophys. Acta, 1141, 262-268.
41. Burbaev, D. Sh., Moroz, I. A., Kotlyar, A. B., Sled, V. D., and Vinogradov, A. D. (1989) FEBS Lett., 254, 47-51.
42. Lee, C. P., and Ernster, L. (1967) Meth. Enzymol, 10, 543-548.
43. Hatefi, Y., and Rieske, J. S. (1967) Meth. Enzymol., 10, 225-231.
44. King, T. E. (1967) Meth. Enzymol., 10, 202-208.
45. Vinogradov, A. D., and King, T. E. (1979) Meth. Enzymol., 55, 118-127.
46. Wan, Y.-P., Williams, R. H., Folker, K., Leung, K. H., and Racker, E. (1975) Biochem. Biophys. Res. Commun., 63, 11-15.
47. Schatz, G., and Racker, E. (1966) J. Biol. Chem., 241, 1429-1437.
48. Lawford, H. G., and Garland, P. B. (1971) Biochem. J., 130, 1029-1044.
49. Ragan, C. I., and Hinkle, P. C. (1975) J. Biol. Chem., 250, 8472-8480.
50. Helfenbaum, L., Ngo, A., Ghelli, A., Linnane, A. W., and Degli Esposti, M. (1997) J. Bioenerg. Biomembr., 29, 71-80.
51. Fowler, L. R., and Richardson, S. H. (1963) J. Biol. Chem., 238, 456-463.
52. Ragan, C. I., and Heron, C. (1978) Biochem. J., 174, 783-790.
53. Mitchell, P. (1975) FEBS Lett., 56, 1-6.
54. Degli Esposti, M., Chelli, A., Crimi, M., Estronell, E., Fato, R., and Lenaz, G. (1993) Biochem. Biophys, Res. Commun., 190, 1090-1096.
55. Degli Esposti, M., Crimi, M., and Ghelli, A. (1994) Biochem. Soc. Trans., 22, 209-212.
56. Tan, A. K., Ramsay, R. R., Singer, T. P., and Miyoshi, H. (1993) J. Biol. Chem., 268, 19328-19333.
57. Morgan-Hughes, J. A., Shapira, A. H. V., Cooper, J. M., Holt, I. J., Harding, A. E., and Clark, J. B. (1990) Biochim. Biophys. Acta, 1018, 217-222.
58. Estronell, E., Fato, R., Pallotti, F., and Lenaz, G. (1993) FEBS Lett., 332, 127-131.
59. Genova, M. L., Castelluccio, C., Fato, R., Parenti Castelli, G., Merlo Pich M., Formiggini, G., Bovina, C., Marchetti, M., and Lenaz, G. (1995) Biochem. J., 311, 105-109.
60. Singer, T. P. (1974) Meth. Biochem. Anal., 22, 123-175.
61. Ohnishi, T., Ragan, C. I., and Hatefi, Y. (1985) J. Biol. Chem., 260, 2782-2788.
62. Dooijewaard, G., and Slater, E. C. (1976) Biochim. Biophys. Acta, 440, 1-15.
63. Dooijewaard, G., and Slater, E. C. (1976) Biochim. Biophys. Acta, 440, 16-35.
64. Hatefi, Y., and Galante, Y. M. (1977) Proc. Natl. Acad. Sci. USA, 74, 846-850.
65. Gavrikova, E. V., Grivennikova, V. G., Sled, V. D., Ohnishi, T., and Vinogradov, A. D. (1995) Biochim. Biophys. Acta, 1230, 23-30.
66. Hinkle, P. C., Butow, R. A., Racker, E., and Chance, B. (1967) J. Biol. Chem., 242, 5169-5173.
67. Boveris, A., and Cadenas, E. (1975) FEBS Lett., 54, 311-314.
68. Chance, B., Sies, H., and Boveris, A. (1979) Physiol. Rev., 59, 527-605.
69. Turrens, J. F., and Boveris, A. (1980) Biochem. J., 191, 421-427.
70. Massey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman, M., and Sullivan, P. A. (1969) Biochem. Biophys. Res. Commun, 36, 891-897.
71. Fridovich, I. (1974) Adv. Enzymol., 41, 35-97.
72. Kotlyar, A. B., Sled, V. D., Burbaev, D. Sh., Moroz, I. A., and Vinogradov, A. D. (1990) FEBS Lett., 264, 17-20.
73. Takeshige, K., and Minakami, S. (1979) Biochem. J., 180, 129-135.
74. Kang, D., Narabayashi, H., Sata, T., and Takeshige, K. (1983) J. Biochem. (Tokyo), 94, 1301-1306.
75. Krishnamoorthy, G., and Hinkle, P. (1988) J. Biol. Chem., 263, 17566-17575.
76. Chan, P. C., and Bielski, B. H. J. (1974) J. Biol. Chem., 249, 1317-1319.
77. Chan, P. C., and Bielski, B. H. J. (1980) J. Biol. Chem., 255, 874-876.
78. Halliwell, B. (1987) FASEB J., 1, 358-364.
79. Luft, R. (1994) Proc. Natl. Acad. Sci. USA, 91, 8731-8738.
80. Sled, V. D., Zinich, V. N., and Kotlyar, A. B. (1989) Biokhimiya, 54, 1571-1575.
81. Lee, C. P., Sigmard-Duquesne, N., Hoberman, H., and Ernster, L. (1965) Biochim. Biophys. Acta, 105, 397-408.
82. Ernster, L., Hoberman, H., Howard, R. L., King, T. E., Lee, C. P., Mackler, B., and Sottocasa, G. (1965) Nature, 207, 940-941.
83. Chen, S., and Guillory, R. J. (1985) Biochem. Biophys. Res. Commun., 129, 584-590.
84. Ernster, L., Estabrook, R. W., Hochstein, P., and Orrenius, S. (1987) Chem. Scr., 27, 1-207.
85. Li, R., Bianchet, M. A., Talalay, P., and Amzel, L. M. (1995) Proc. Natl. Acad. Sci. USA, 92, 8846-8850.
86. Sled, V. D., Rudnitzky, N. I., Hatefi, Y., and Ohnishi, T. (1994) Biochemistry, 33, 10069-10075.
87. Sled, V. D., and Vinogradov, A. D. (1993) Biochim. Biophys. Acta, 1143, 199-203.
88. Djavadi-Ohaniance, L., and Hatefi, Y. (1975) J. Biol. Chem., 250, 9397-9403.
89. Rydström, J., Montelius, J., Bäckström, D., and Ernster, L. (1978) Biochim. Biophys. Acta, 501, 370-380.
90. Ragan, C. I., Widger, W. R., and King, T. E. (1974) Biochem. Biophys. Res. Commun., 3, 894-900.
91. Löw, H., and Vallin, I. (1963) Biochim. Biophys. Acta, 69, 361-374.
92. Bakker, P. T. A., and Albracht, S. P. J. (1986) Biochim. Biophys. Acta, 850, 413-422.
93. Van Belzen, R., and Albracht, S. P. J. (1989) Biochim. Biophys. Acta, 974, 311-320.
94. Van Belzen, R., Van Gaalen, M. C. M., Cuypers, P. A., and Albracht, S. P. J. (1990) Biochim. Biophys. Acta, 1017, 152-159.
95. Albracht, S. P. J., and de Jong, A. M. P. (1997) Biochim. Biophys. Acta, 1318, 92-106.
96. Glinn, M. A., Lee, C. P., and Ernster, L. (1997) Biochim. Biophys. Acta, 1318, 246-254.
97. Chen, S., and Guillory, R. J. (1981) J. Biol. Chem., 256, 8318-8323.
98. Deng, P. S. K., Hatefi, Y., and Chen, S. (1990) Biochemistry, 29, 1094-1098.
99. Yagi, T., and Dinh, T. M. (1990) Biochemistry, 29, 5515- 5520.
100. Xu, X.-M., and Yagi, T. (1991) Biochem. Biophys. Res. Commun., 174, 667-672.
101. Preis, D., Van der Pas, J. C., Nehls, U., Röhlen, D.- A., Sackmann, U., Jahnke, U., and Weiss, H. (1991) Biochim. Biophys. Acta, 1089, 389-390.
102. Röhlen, D. A., Hoffmann, J., Van der Pas, J. C., Nehls, U., Preis, D., Sackman, U., and Weiss, H. (1991) FEBS Lett., 278, 75-78.
103. Clark, W. M. (1960) Oxidation Reduction Potentials of Organic Systems, Williams and Wilkins, Baltimore.
104. Sanadi, D. R., and Fluharty, A. L. (1963) Biochemistry, 2, 523-528.
105. Grivennikova, V. G., Gavrikova, E. V., Timoshin, A. A., and Vinogradov, A. D. (1993) Biochim. Biophys. Acta, 1140, 282-292.
106. Sucheta, A., Ackrell, B. A. C., Cochran, B., and Armstrong, F. A. (1992) Nature, 356, 361-362.
107. Grivennikova, V. G., and Vinogradov, A. D. (1982) Biochim. Biophys. Acta, 682, 491-495.
108. Tushurashvili, P. R., Gavrikova, E. V., Ledenev, A. N., and Vinogradov, A. D. (1985) Biochim. Biophys. Acta, 809, 145-159.
109. Chance, B., and Hollunger, G. (1960) Nature, 185, 666-672.
110. Klingenberg, M., and Slenczka, W. (1959) Biochem. Z., 331, 486-517.
111. Proc. Fifth Int. Congr. of Biochemistry (1963) Vol. 5, Pergamon Press, Oxford, London, New York, Paris.
112. Chance, B. (ed.) (1963) Energy-Linked Functions of Mitochondria, Academic Press, New York.
113. Beyer, R. (1967) Meth. Enzymol., 10, 186-196.
114. Thorn, M. B. (1962) Biochem. J., 85, 116-127.
115. Kotlyar, A. B., and Vinogradov, A. D. (1984) Biochim. Biophys. Acta, 784, 24-34.
116. Ackrell, B. A. C., Kearney, E. B., and Edmondson, D. E. (1975) J. Biol. Chem., 250, 7114-7119.
117. Vasilyeva, E. A., Minkov, I. B., Fitin, A. F., and Vinogradov, A. D. (1982) Biochem. J., 202, 9-14.
118. Vasilyeva, E. A., Fitin, A. F., Minkov, I. B., and Vinogradov, A. D. (1980) Biochem. J., 188, 807-815.
119. Ernster, L., Carlsson, C., Hundal, T., and Nordenbrand, K. (1979) Meth. Enzymol, 55, 399-407.
120. Panchenko, M. V., and Vinogradov, A. D. (1985) FEBS Lett., 184, 226-230.
121. Hommes, F. A. (1963) Biochim. Biophys. Acta, 77, 173- 182.
122. Racker, E., and Horstman, L. (1967) J. Biol. Chem., 242, 2547-2556.
123. Kotlyar, A. B., and Gutman, M. (1992) Biochim. Biophys. Acta, 1140, 169-174.
124. Grivennikova, V. G., Maklashina, E. O., Gavrikova, E. V., and Vinogradov, A. D. (1997) Biochim. Biophys. Acta, 1319, 223-232.
125. Boyer, R. E. (1967) Meth. Enzymol., 10, 186-194.
126. Lee, C. P. (1979) Meth. Enzymol., 55, 105-112.
127. Huang, C. H., Keyhani, E., and Lee, C. P. (1973) Biochim. Biophys. Acta, 305, 455-463.
128. Huang, C. H., and Lee, C. P. (1975) Biochim. Biophys. Acta, 376, 398-414.
129. Teixeira da Cruz, A., Rydström, J., and Ernster, L. (1971) Eur. J. Biochem., 23, 203-211.
130. Rydström, J., Teixeira da Cruz, A., and Ernster, L. (1971) Eur. J. Biochem., 23, 212-219.
131. Lenaz, G. (1998) Biochim. Biophys. Acta, 1364, 207-221.
132. Hatefi, Y., Haavik, A. G., and Griffiths, D. E. (1962) J. Biol. Chem., 237, 1676-1680.
133. Hatefi, Y., and Rieske, J. S. (1967) Meth. Enzymol., 10, 239-245.
134. Ragan, C. I., and Racker, E. (1973) J. Biol. Chem., 248, 2563-2569.
135. Guénebaut, V., Vincentelli, R., Mills, D., Weiss, H., and Leonard, K. R. (1997) J. Mol. Biol., 265, 409-418.
136. Galante, Y., and Hatefi, Y. (1978) Meth. Enzymol., 53, 15-21.
137. Finel, M., Majander, A. S., Tyynelä, J., de Jong, A. M. P., Albracht, S. P. J., and Wikström, M. (1994) Eur. J. Biochem., 226, 237-242.
138. Buchanan, S. K., and Walker, J. E. (1996) Biochem. J., 318, 343-349.
139. Galante, Y., and Hatefi, Y. (1979) Arch. Biochem. Biophys., 192, 559-568.
140. Lazdunski, M., Petitclere, D., Chappelet, D., and Lazdunski, C. (1971) Eur. J. Biochem., 20, 124-135.
141. Slater, E. C. (1950) Biochem. J., 46, 499-503.
142. Morrison, R. O., and King, T. E. (1962) Biochemistry, 1, 1017-1024.
143. Minakami, S., Schindler, F. J., and Estabrook, R. W. (1964) J. Biol. Chem., 239, 2049-2054.
144. Luzikov, V. N., Saks, V. A., and Berezin, I. V. (1970) Biochim. Biophys. Acta, 223, 16-30.
145. Luzikov, V. N., and Romashina, L. V. (1972) Biochim. Biophys. Acta, 267, 37-47.
146. Saks, V. A., Kupriyanov, V. V., and Luzikov, V. N. (1972) Biochim. Biophys. Acta, 283, 42-53.
147. Redfearn, E. R., Whittaker, P. A., and Burgos, J. (1965) in Oxidases and Related Redox Systems (King, T. E., Mason, H. S., and Morrison, M., eds.) John Wiley and Sons, Inc., New York, pp. 943-959.
148. Minakami, S., Schindler, F. J., and Estabrook, R. W. (1964) J. Biol. Chem., 239, 2042-2048.
149. Estabrook, R. W., Tyler, D. D., Gonze, J., and Peterson, J. A. (1968) in Flavins and Flavoproteins (Yagi, K., ed.) University of Tokyo Press, Tokyo, pp. 268-279.
150. Kotlyar, A. B., Sled, V. D., and Vinogradov, A. D. (1992) Biochim. Biophys. Acta, 1098, 144-150.
151. Maklashina, E. O., Sled, V. D., and Vinogradov, A. D. (1994) Biochemistry (Moscow), 59, 707-714 (Russ.).
152. Erecinska, M., and Wilson, D. F. (1967) Arch. Biochem. Biophys., 174, 143-157.
153. Maklashina, E. O., and Vinogradov, A. D. (1994) Biochemistry (Moscow), 59, 1221-1226 (Russ.).
154. Dolphin, D., Poulson, R., and Avramovic, O. (eds.) (1989) Glutathione: Chemical, Biochemical and Medical Aspects, John Wiley and Sons, New York.
155. Syroeshkin, A. V., Vasilyeva, E. A., and Vinogradov, A. D. (1995) FEBS Lett., 366, 29-32.
156. De Jong, A. M. P., and Albracht, S. P. J. (1994) Eur. J. Biochem., 222, 975-982.
157. Van Beizen, R., Kotlyar, A. B., Moon, N., Dunham, R., and Albracht, S. P. J. (1997) Biochemistry, 36, 886- 893.
158. Schneider, K., Patil, D. S., and Cammack, R. (1983) Biochim. Biophys. Acta, 748, 353-361.
159. Sun, J.-H., and Arp, D. J. (1991) Arch. Biochem. Biophys., 287, 225-233.
160. Ferber, D. M., Moy, B., and Maier, R. (1995) Biochim. Biophys. Acta, 1229, 334-346.