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Field Enhanced Spin Transport in Frustrated Hemoglobin, Hemi along the Fe- N symmetric Axis

Gizachew Diga Milki

Abstract


Spin transport in frustrated/topological structures is seen as free transport or field enhanced transport. The subject of transport is therefore either the movement of actual material or charge carrier and spin along a conductor. In physical point of view this phenomena seen as field assisted spin transport or thermal energy enhanced charge carriers transport along the frustrated systems, nanowires or conductors. Hence, the actions of electric fields, magnetic fields and temperature are focused. This research therefore, highlights the phenomena of such transport along the specialized system, frustrated system and/or topological system. Hence the transport like billiard or ballistic like transports are visualized in frustrated crystal system like proteins, hemoglobin. In this paper, the nature of field enhanced spin transport in Myoglobin (Mgb), where the electron donor is oxygen in the red blood cell and the role in establishing spin transport and of Fe in establishing the magnetic state is presented. This transport is visualized by assuming the Hemoglobin as frustrated and topology system.


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References


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Martha H. Redi et al., hemoglobin-carbon monoxide binding rate low temperature magneto-optical detection of spin tunneling, Biophys.1981, V.35, 471- 484

Selam Mayda et al. (2020) 10:8569

Kara. L. Brena, Richard Eisenberga, and Harry B. Gray, (2015) Vol. 112, №. 43. 13123–13127.

Markus Meuwly, and Martin Karplus, the functional role of the hemoglobin-water

interface (2021), 80, CH- 4056

M. Z. Hasan and C. L. Kane, Colloquium: Topological insulators, 2010. Rev. Mod. Phys. 82 3045 - 3067

J E Moore, the birth of topological insulators Nature, (2010) 464, 194 -198

Frederic G. Hirsch et al. electrical conductivity of blood, (2022) 5. 11, 1017- 1033

Heinrich Roder, et al., Comparison of the magnetic properties of deoxy- and

photo dissociated myoglobin, 1984, Vol. 81, PP. 2359-2363

A. M. Visuri, et, al., “Spin transport in a one-dimensional quantum wire” Physical review Research. 2020; 2: 023062.

Todde, Hovmöller, Laaksonen, “Influence of antifreeze proteins on the ice/water interface” Journal of Physical Chemistry B. 2015; 119(8): 3407-3413.

Paoli, M. Marles Wright. J., Smith A. “Structure function relationships in hemi proteins”. DNA and cell biology. 2002; 21(4): 271-280.

H. Richard Leuchtag. “Laser research” Physics Today. November 1975; 28(11): 55.

Qipeng Tian, Shijie Xie. “Spin Injection and Transport in Organic Materials, Micromachines 2019, 10(90: 596.

Chris Higgins Little Acre, Main Road Shurdington Nr Cheltenham, 2005

F. C.Wireko & D. J. Abraham. X-ray diffraction study of the binding of the antisickling agent 12C79 to human hemoglobin”. Proceedings of the National Academy of Sciences of the United States of America. 1991; 88(6): 2209- 2211.

Alan N. Schechter, blood, 2008. V. 112, № .10

Scheidt, W. R. & Gouterman, M. (1983) in Iron Porphyrins, eds. Lever, A. B. P. & Gray, H. B. (Addison-Wesley, Reading, MA), Part 1, pp. 89-139.

Prof. A. Gamgee, on behavior of oxyhemoglobin, Victoria University, (1901).

Herbert Sheinberg et al, Differential titration by means of paper electrophoresis and the structure of human hemoglobin, (1954). Vol. 40,

Huang Y. X, Wu Z-J, Huang B-T, Luo M, Pathway and mechanism of PH dependent human hemoglobin tetramer-dimer-monomer, dissociations. 2013.8. (11), e81708

Gunhild Layer et al., Structure and function of enzymes in heme biosynthesis, Protein Science, 2010 VOL 19:1137- 1161

W. H. Freeman, protein composition, and structure, 2007, 6th edi

F. J. W. Roughwn, Kinetics of gas transport in blood, 2016, Vol. 19 No. 1

Sarah E. J. Bowman and Kara L. Bren, the Chemistry and Biochemistry of Hemi c: Functional Bases for Covalent Attachment, Nat Prod Rep. 2008, 25(6): 1118–1130.

Vanja Maric et al. Resilience of the topological phases to frustration, nature portfolio (2021) 11:6508

Ferreiro et al., frustration in biomolecules, Rev. biophysics, 2014, 47(4): 285–363

Zhendong Fu, Spin Correlations and Excitations in Spin-frustrated Molecular and Molecule-based Magnets, 2012, V.43, 1866-1807

S. Sanvito∗ and A. R. Rocha, Molecular-Spintronics, Journal of Computational and Theoretical Nanoscience, (2006) DOI: 10.1166/jctn.2006.3047

Roderich Moessner and Aurther P Ramirez, Geometrical frustration, physics today 59, 2, 24 (2006)

Dixit A, Verkhivker GM, the Energy Landscape Analysis of Cancer Mutations in Protein Kinases. PLoS. (2011), 1. 6(10)

Kees M. Schep, Pauli J. Kelly, Gerrit E. W. Bauer, 1998, Phy. Rev.57. 15, 8907

Sayak Subhra Panda et al., Solid-state electrical applications of protein and peptide based nanomaterials, Chem. Soc. Rev., 2019,48, 5616-5616

A.Y. Kasumov, M. Kodiak, S. Guerin, B. Reulet, V.T. Tolko, D.V. Klinov, H. Bouchiat, Science 291 (2001) 280.

Sabyasachi Mukhopadhyay et al. Solid-State Protein Junctions, I. Science, (2020) 23, 101099, 22

Shiro Takashima, the dielectric properties of hemoglobin, 1957, V. 80, 4474 - 4475.

Mengwei Si et al., ferroelectric semiconductor field effect transistor, 2017, 1812 - 02933

Wiebe Wagemans and Bert Koopmans, spin transport & MR organic semiconductors, phy. status of solid, (2011). 248. № 5, 1029 -1041

Youxun Liu et al. Selective Removal of Hemoglobin from Blood Using , Int. BMR, 2017 Volume 11, Article ID 7309481

Robert E. Ulanowicz and George Frazier JR, the transport of oxygen and carbon dioxide in hemoglobin system, (1970), 7, 111-129

R. A. Caetano, Spin-Current and Spin-Splitting in Helicoidally Molecules due to spin orbit Coupling Scientific Reports , 2015, 6:23452

L. Kubisz, D. Hojan Jezierska DC, electrical Conductivity in Studies on Solid–State Proteins, (2010), V. 118, 1, pp. 103-105.

Barnett Rosenberg, electrical conductivity of proteins, Nature (1962). V. 193, pages3 64–365

Y. Abdullah et al., Synthesis and Characterization of Manganese Doped

ZnO Nanoparticles, Int. J. Basic & Applied Sciences IJBAS-IJENS (2011) Vol: 11 No: 04

Solomon Adugna et al, Amino acids and Proteins, 2004, No 663-A-00-00-0358-00, PP.105-159

George Datseris, Lukas Hupe and Ragnar Fleischmann Estimating Lyapunov exponents in billiard chaos, 2019. 29, 093115

Ye Xue, Samuel Lofland, and Xiao Hu, Thermal Conductivity of Protein-Based Materials, Polymers, 2019, 11, 456

Linus Pauling & Charles D. Coryell, The magnetic properties and structure of hemoglobin, oxyhemoglobin and carbonmonoxyhemoglobin (1936), V. 22, 210–217

Alaa Eldin F. Nasser and James F. Rustling J. Am. Chem. 1996, 118, 3043-3044

Kees M. Schep et al., ballistic transport and electronic structure phy. rev. B, 1998, V. 57, pp. 8907 -8926.

Linus Pauling; Magnetic and structure properties of oxyhemoglobin, Proc. Nati. Acad. Sci. USA, 1977. Vol. 74, No. 7, PP. 2612-2613

Daniel M. Free, et al., conformation exchange in membrane transport of protein altered by protein crystals, 2010 V. 99. 1604-1610.

Liu Zhang Qi, the Quantum Anomalous Hall Effect: Theory and Experiment Annu. Rev. Condens. Matter Phys. 2016. 7: 301-21

Izhar Rona, Lior Sepunaroa, Stella Izhakova, Noga Friedmanb, Israel Pechtc, Mordechai Shevesb, and David Cohen, Weizmann Institute of Science, POB 2. 6, Rehovot 76100

Jai-Yule Kong, Osato Miyawaki, Kozo Nakamura, Toshimasa Yano, Agricultural and Biological Chemistry, Volume 46, Issue 3, 1 March 1982, Pages 789 - 794.

Martha H. Redi et al., hemoglobin-carbon monoxide binding rate low temperature magneto-optical detection of spin tunneling, Biophys.1981, V.35, 471- 484

Selam Mayda et al. (2020) 10:8569

Kara. L. Brena, Richard Eisenberga, and Harry B. Gray, (2015) Vol. 112, №. 43. 13123–13127.

Markus Meuwly, and Martin Karplus, the functional role of the hemoglobin-water

interface (2021), 80, CH- 4056

M. Z. Hasan and C. L. Kane, Colloquium: Topological insulators, 2010. Rev. Mod. Phys. 82 3045 - 3067

J E Moore, the birth of topological insulators Nature, (2010) 464, 194 -198

Frederic G. Hirsch et al. electrical conductivity of blood, (2022) 5. 11, 1017- 1033

Heinrich Roder, et al., Comparison of the magnetic properties of deoxy- and

photo dissociated myoglobin, 1984, Vol. 81, PP. 2359-2363


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