Quantum Chemical Studies of the Myosin ATPase Mechanism

Kagawa, Hiroshi

doi:10.1272/jnms.74.4

Cited by 2 publications

(9 citation statements)

References 40 publications

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“…The structures used in this study are constructed from the following X-ray coordinate files in the PDB: 1MMD [9] and 1VOM [10]. 1MMD, which was used in previous studies by Kagawa and Mori [4,5], is the 3D structure of the myosin motor domain of Dictyostelium discoideum myosin II with an ATP analog, ADPBeF 3 . 1VOM, which is used in combination with 1MMD in the present study, has a structure almost identical to that of 1MMD but uses another analog, ADPVO 4 .…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Kagawa et al studied the structure of adenosine triphosphate (ATP) by using the PM3 method in the MOPAC computer program [1][2][3]. Furthermore, Kagawa and Mori studied the initial process of ATP hydrolysis in the myosin motor domain using the PM3 algorithm in MOPAC97 [4,5]. Analyzing the electronic states of the model structure by means of a molecular orbital correlation diagram, they considered that (A) H 2 O(1181) corresponds to lytic water and (B) the highest occupied molecular orbitals (HOMOs) indicate that nonbridging O atoms of γ-phosphate constitute the reaction site of ATP hydrolysis in the model structure.…”

Section: Introductionmentioning

confidence: 99%

“…They also studied the effect of the amino acid charge and reported the relation between the inorganic phosphate charge and the phosphate structure [6]. Subsequently, Kagawa reviewed quantum studies on myosin-based ATP hydrolysis [7].…”

Section: Introductionmentioning

confidence: 99%

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Molecular Orbital Study of the Interaction between MgATP and the Myosin Motor Domain Using the PM6 Method

Kagawa

Kikuchi

Gao

et al. 2010

J. Comput. Chem. Jpn.

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Dedicated to the late Prof. Kazuhide MORI. Previously, our research group carried out molecular orbital studies of the interaction between MgATP and the myosin motor domain using the PM3 method of MOPAC97. In this study, we present recalculation results obtained using the PM6 method of MOPAC2009 and discuss the problems that may be encountered in further studies. Previous research carried out by our group in this field is introduced briefly. Furthermore, it is proposed that the increase in the distance between P γ and the bridging O atom bound to P β initiates the dissociation of γ-phosphate from ATP. Our results demonstrate that semi-empirical molecular orbital methods are useful in studying the chemical reactions underlying the initial step of ATP hydrolysis in the myosin motor domain.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Molecular Orbital Study of the Interaction between MgATP and the Myosin Motor Domain Using the PM6 Method

Kagawa

Kikuchi

Gao

et al. 2010

J. Comput. Chem. Jpn.

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“…Moreover, a high ratio, increased [H + ], and excessive heat, given off as a result of the splitting of the ATP terminal bond during strenuous activity, may reduce the free energy provided by a given molecule of ATP during hydrolysis. The net effect amounts to a reduction in free energy available for optimal repositioning of the crossbridge heads at the end of the contraction cycle and before activation [23‐27]. By this mechanism, declines in crossbridge function may include slowing of repositioning and/or suboptimal alignment of the myosin head to an angle of pull on the thin filament that reduces the force generated by the power stroke (Table 2).…”

Section: Introductionmentioning

confidence: 99%

Peripheral Fatigue: High‐Energy Phosphates and Hydrogen Ions

Keyser

2010

PM&R

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Peripheral fatigue results from an overactivity-induced decline in muscle function that originates from non-central nervous system mechanisms. A common symptom of fatigue is a feeling of tiredness or weariness because of overexertion, such as that associated with intense or prolonged physical exercise. Fatigue is worsened by low physical fitness and chronic illnesses. These conditions may intensify fatigue to levels that limit physical and social functioning and severely diminish health-related quality of life. Although etiologic aspects of peripheral fatigue are often associated with regulatory system (neurologic, endocrine, immunologic, muscular) and support system (cardiovascular, pulmonary, metabolic, renal, digestive, skeletal) limitations, final mediation occurs in muscle cells as a result of altered crossbridge functioning. Specifically, the final product and ionic metabolite accumulation that result from adenosine triphosphate hydrolysis appear to inhibit crossbridge formation and activation. Thus, clinical manifestations of peripheral fatigue often can be observed as limitations placed upon muscle or cardiorespiratory endurance, here defined as fatigue resistance. An overview of the common pathways by which peripheral fatigue can be mediated is provided. Product inhibition of contractile chemistry is brought into focus as a common pathway through which the mechanisms of peripheral fatigue often act.

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Quantum Chemical Studies of the Myosin ATPase Mechanism

Cited by 2 publications

References 40 publications

Molecular Orbital Study of the Interaction between MgATP and the Myosin Motor Domain Using the PM6 Method

Molecular Orbital Study of the Interaction between MgATP and the Myosin Motor Domain Using the PM6 Method

Peripheral Fatigue: High‐Energy Phosphates and Hydrogen Ions

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