The met and deoxy forms of sperm whale myoglobin (Mb) can be unfolded by guanidine hydrochloride (GuHCl). Electronic absorption and circular dichroism spectroscopic measurements show that folded deoxyMb is more stable than the folded met protein. Laser excitation of NADH generates species that rapidly reduce unfolded metMb, triggering the formation of folded deoxyMb in less than 10 ms (pH 7.0, 2.5 to 3 M GuHCl, 20 ℃). At comparable reaction driving forces (～10 kJ/mol), deoxyMb folds much faster than reduced cytochrome c.
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机译：抹香鲸肌红蛋白（Mb）的遇合形式和脱氧形式可以通过盐酸胍（GuHCl）展开。电子吸收和圆二色性光谱测量表明，折叠的脱氧Mb比折叠的met蛋白更稳定。 NADH的激光激发产生的物种会迅速还原未折叠的metMb，并在不到10毫秒（pH 7.0、2.5至3 M GuHCl，20℃）中触发折叠的脱氧Mb的形成。在相当的反应驱动力（〜10 kJ / mol）下，脱氧Mb的折叠速度比还原的细胞色素c快得多。
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