Muonium and Water in Histidine Amino Acid

In order to apply muon spin rotation and relaxation method for study of life sciences like electron transfer process, detection of molecular concentration, photosynthesis process, etc., theoretical study to understand the stopping sites of muon and its charge species in the macromolecules is necessary. In the systematic theoretical study to know the behaviour of muon and muonium in water hydrated biological macromolecules like protein and DNA through the first-principles approach, the behaviour of a water molecule in the presence of muonium in histidine amino acid with extended main chain is presented here. The sites of a water molecule and a muonium in histidine amino acid are estimated. Two possible sites with potential energy 0.3 eV (approximately) for water molecule in the optimized structure of muonium in extended main chain histidine were estimated. Water in the sites is expected to contribute to enhance the intra- and inter-chain electron transfer in the system as reported experimentally.

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Intra- and inter-molecular electron transfer in cytochrome c and myoglobin observed by the muon spin relaxation method

Physica B Condensed Matter ◽

10.1016/s0921-4526(00)00298-2 ◽

2000 ◽

Vol 289-290 ◽

pp. 631-635 ◽

Cited By ~ 18

Author(s):

K Nagamine ◽

F.L Pratt ◽

S Ohira ◽

I Watanabe ◽

K Ishida ◽

...

Keyword(s):

Electron Transfer ◽

Cytochrome C ◽

Spin Relaxation ◽

Muon Spin ◽

Relaxation Method ◽

Muon Spin Relaxation ◽

Molecular Electron

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Microscopic behavior of positively charged particles in solid hydrogen by the muon spin rotation and relaxation method

Physical Review B ◽

10.1103/physrevb.60.6484 ◽

1999 ◽

Vol 60 (9) ◽

pp. 6484-6494

Author(s):

W. Higemoto ◽

K. Satoh ◽

N. Nishida ◽

K. Nishiyama ◽

K. Nagamine

Keyword(s):

Muon Spin ◽

Charged Particles ◽

Relaxation Method ◽

Solid Hydrogen ◽

Spin Rotation ◽

Muon Spin Rotation ◽

Positively Charged

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Amino acid and cinnamaldehyde conjugated Schiff bases as proficient corrosion inhibitors for mild steel in 1 M HCl at higher temperature and prolonged exposure: Detailed electrochemical, adsorption and theoretical study

Journal of Molecular Liquids ◽

10.1016/j.molliq.2020.115077 ◽

2021 ◽

Vol 324 ◽

pp. 115077

Author(s):

Sanjoy Satpati ◽

Aditya Suhasaria ◽

Subhas Ghosal ◽

Abhijit Saha ◽

Sukalpa Dey ◽

...

Keyword(s):

Amino Acid ◽

Mild Steel ◽

Schiff Bases ◽

Corrosion Inhibitors ◽

Theoretical Study ◽

Prolonged Exposure ◽

Higher Temperature ◽

Electrochemical Adsorption

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Theoretical Study of the Binding of the Thiol-Containing Cysteine Amino Acid to the Silver Surface Using a Cluster Model

The Journal of Physical Chemistry A ◽

10.1021/acs.jpca.0c11182 ◽

2021 ◽

Vol 125 (16) ◽

pp. 3244-3256

Author(s):

Pham Vu Nhat ◽

Nguyen Thanh Si ◽

Nguyen Thanh Tien ◽

Minh Tho Nguyen

Keyword(s):

Amino Acid ◽

Cluster Model ◽

Theoretical Study ◽

Silver Surface ◽

Cysteine Amino Acid

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Fe(2)OG: an integrated HMM profile-based web server to predict and analyze putative non-haem iron(II)- and 2-oxoglutarate-dependent dioxygenase function in protein sequences

BMC Research Notes ◽

10.1186/s13104-021-05477-z ◽

2021 ◽

Vol 14 (1) ◽

Author(s):

Siddhartha Kundu

Keyword(s):

Amino Acid ◽

Water Molecule ◽

Active Site ◽

Ferrous Iron ◽

Web Server ◽

Protein Sequences ◽

Diverse Group ◽

And Function ◽

Functionally Diverse ◽

Haem Iron

Abstract Objective Non-haem iron(II)- and 2-oxoglutarate-dependent dioxygenases (i2OGdd), are a taxonomically and functionally diverse group of enzymes. The active site comprises ferrous iron in a hexa-coordinated distorted octahedron with the apoenzyme, 2-oxoglutarate and a displaceable water molecule. Current information on novel i2OGdd members is sparse and relies on computationally-derived annotation schema. The dissimilar amino acid composition and variable active site geometry thereof, results in differing reaction chemistries amongst i2OGdd members. An additional need of researchers is a curated list of sequences with putative i2OGdd function which can be probed further for empirical data. Results This work reports the implementation of $$Fe\left(2\right)OG$$ F e 2 O G , a web server with dual functionality and an extension of previous work on i2OGdd enzymes $$\left(Fe\left(2\right)OG\equiv \{H2OGpred,DB2OG\}\right)$$ F e 2 O G ≡ { H 2 O G p r e d , D B 2 O G } . $$Fe\left(2\right)OG$$ F e 2 O G , in this form is completely revised, updated (URL, scripts, repository) and will strengthen the knowledge base of investigators on i2OGdd biochemistry and function. $$Fe\left(2\right)OG$$ F e 2 O G , utilizes the superior predictive propensity of HMM-profiles of laboratory validated i2OGdd members to predict probable active site geometries in user-defined protein sequences. $$Fe\left(2\right)OG$$ F e 2 O G , also provides researchers with a pre-compiled list of analyzed and searchable i2OGdd-like sequences, many of which may be clinically relevant. $$Fe(2)OG$$ F e ( 2 ) O G , is freely available (http://204.152.217.16/Fe2OG.html) and supersedes all previous versions, i.e., H2OGpred, DB2OG.

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