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. Author manuscript; available in PMC: 2010 Apr 28.
Published in final edited form as: Biochemistry. 2009 Apr 28;48(16):3658–3668. doi: 10.1021/bi802339c

Table 1.

Time Constants of Molecular Dynamics, Protein Motion and Catalysisa

Time sec
s 1 common kcat range
ms 10−1
10−2 kcat PNP
10−3 flap opening TIM kchem PNP
μs 10−4 rate O2 Hb to deoxy Hb loop motion PNP
10−5 flap closing OPRTase and PTPase domain motion in protein
10−6
ns 10−7 substrate/ligand binding PNPb
10−8 rotation/translation for NACs catalytic site capture limita
10−9
ps 10−10 H2O diffuses two diameters
10−11 collisionless H+ ion transfer
10−12 light travels 0.3 mm
fs 10−13 bond vibration; TS lifetime
10−14 TS PNPc
10−15
a

Modified from ref (18).

b

From ref (38).

c

From ref (17).