Premium
Assay conditions for the mitochondrial NADH:coenzyme Q oxidoreductase
Author(s) -
Estornell Ernesto,
Fato Romana,
Pallotti Francesco,
Lenaz Giorgio
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80498-j
Subject(s) - coenzyme q – cytochrome c reductase , cofactor , chemistry , biochemistry , reductase , mitochondrion , coenzyme a , electron acceptor , oxidoreductase , enzyme , stereochemistry , combinatorial chemistry , cytochrome c
The assay of Complex I activity requires the use of artificial acceptors, such as short‐chain coenzyme Q homologs and analogs, because the physiological quinones, such as CoQ 10 , are too insoluble in water to be added as substrates to the assay media. The medical interest raised in the last years on the pathological changes of Complex I activity has focussed on the requirement of easy reliable assays for its analysis. We have undertaken a systematic examination of the assay conditions of Complex I in mitochondrial membranes, using a series of quinones as electron acceptors, particularly the coenzyme Q homologs CoQ 0 , CoQ 1 and CoQ 2 , and the analogs duroquinone and decylubiquinone. Our findings have pointed out that the most suitable electron acceptor for the NADH:CoQ reductase assay is the homolog CoQ 1 . The analog DB, commercially available, although yielding a high activity, nevertheless causes some problems for the standardization of the assay conditions.