1. A Missense Mutation of Cytochrome Oxidase Subunit II Causes Defective Assembly and Myopathy 
Shamima Rahman, Jan-Willem Taanman, J. Mark Cooper, Isabelle Nelson, Ian Hargreaves, Brigitte Meunier, Michael G Hanna, José J. García, Roderick A. Capaldi, Brian D. Lake, James V. Leonard, Anthony H.V. Schapira 
The American Journal of Human Genetics 
Volume 65, Issue 4, Pages (October 1999)
DOI: /302590
Copyright © 1999 The American Society of Human Genetics Terms and Conditions

2. Figure 1
COX-activity staining (panels A and B) and COX immunohistochemical staining (panels C–H) in muscle. A = control; B = patient; C = COX subunit II (control); D = COX subunit II (patient); E = COX subunit I (patient); F = COX subunit IV (patient); G = COX subunit Va (patient); and H = COX subunit VIc (patient). Control sections stained for subunits I, IV, Va, and VIc appeared the same as section C.
The American Journal of Human Genetics  , DOI: ( /302590)
Copyright © 1999 The American Society of Human Genetics Terms and Conditions

3. Figure 2
Immunoblot analysis of skeletal muscle mitochondrial fractions, from the patient (P) and two controls (C). Blots were developed with subunit-specific monoclonal antibodies to COX subunits, the flavoprotein subunit of SDH (SDH Fp), core protein 1 of complex III (core 1), the α subunit of F1-ATP synthase (F1-α), and VDAC.
The American Journal of Human Genetics  , DOI: ( /302590)
Copyright © 1999 The American Society of Human Genetics Terms and Conditions

4. Figure 3
Flash photolysis and recombination spectra of the CO-ferroheme a3 compound of dissolved muscle mitochondria, from the patient and a control. After reduction by sodium dithionite and treatment with CO, laser-flash photolysis and recombination of CO was monitored at nm versus time.
The American Journal of Human Genetics  , DOI: ( /302590)
Copyright © 1999 The American Society of Human Genetics Terms and Conditions

5. Figure 4
Sequence chromatogram of mitochondrial COX II gene, in control sequence (top) and patient's sequence (bottom). The arrow indicates mutated base (adenine in place of wild-type thymine).
The American Journal of Human Genetics  , DOI: ( /302590)
Copyright © 1999 The American Society of Human Genetics Terms and Conditions

6. Figure 5
Alignment of amino acid sequence in COX subunit II (mitochondrial genome sequence data obtained from gopher directory at the Molecular Evolution and Organelle Genomics web site). The large box represents the first α-helical region in the bovine structure (Tsukihara et al. 1996). The mutation in our patients involves amino acid residue 29.
The American Journal of Human Genetics  , DOI: ( /302590)
Copyright © 1999 The American Society of Human Genetics Terms and Conditions

7. Figure 6
Structure of monomer of bovine cytochrome c oxidase. The diagram shows the assembled bovine holoenzyme, with an arrow indicating the site, in subunit II, that is mutated in our patient. The diagram was constructed with use of the data published by Tsukihara et al. (1996) in the Quanta program.
The American Journal of Human Genetics  , DOI: ( /302590)
Copyright © 1999 The American Society of Human Genetics Terms and Conditions