Energy transduction optical sensor in skeletal myosin.
The skeletal myosin cross-bridge in dynamic association with actin is the unitary energy transducer in muscle, converting free energy from ATP hydrolysis into contractile force. Myosin's conserved ATP-sensitive tryptophan (AST) is an energy transduction optical sensor signaling transduction-related transient conformation change by modulating its fluorescence intensity amplitude and relaxation rate. Recently introduced techniques have provided the means of observing the time-resolved intensity decay from this single residue in the native protein to elucidate the mechanism of its ATP sensitivity. AST signal characteristics could be derived from local protein structure by a scenario involving interactions with excited-state tryptophan. This investigation suggests the very different possibility that hypochromism induced in the tryptophan absorption band, a ground-state effect, is a significant structural effector of optical transduction sensing. This possibility makes feasible the interpretation of the transient AST optical signal in terms of dynamical protein structure, thereby raising the empirical signal to the level of a structural determinant. Using the crystallographically based geometry from several myosin structures, the maximum calculated AST hypochromism is <10% to be compared with the value of approximately 30% observed here experimentally. Rationalizing the discrepancy invites further investigation of S1 dynamical structure local to the AST during transduction.
Burghardt
Thomas P
TP
Department of Biochemistry and Molecular Biology, Mayo Foundation, 200 First Street Southwest, Rochester, Minnesota 55905, USA. burghardt@mayo.edu
Park
Sungjo
S
Dong
Wen-Ji
WJ
Xing
Jun
J
Cheung
Herbert C
HC
Ajtai
Katalin
K
D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D015374:Biosensing Techniques; D004735:Energy Transfer; D066298:In Vitro Techniques; D007700:Kinetics; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism; D009119:Muscle Contraction / Q000502:physiology; D018482:Muscle, Skeletal / Q000378:metabolism*; D015879:Myosin Subfragments / Q000737:chemistry / Q000378:metabolism; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism*; D055095:Optics and Photonics; D011487:Protein Conformation; D011817:Rabbits; D015398:Signal Transduction; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry
D000199:Actins; D020409:Molecular Motor Proteins; D015879:Myosin Subfragments; D014364:Tryptophan; D000255:Adenosine Triphosphate; D009218:Myosins