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Nazhmutin Gadzhymagomedovich Abdulaev (Russian: Нажмутин Гаджимагомедович Абдулаев) (January 21, 1941- December 20, 2018), Soviet bioorganic chemist, professor, recipient of the USSR and Russia State Prize in the field of science and engineering. He played a key role in establishing the structures of bacteriorhodopsin, as well as bovine and octopus rhodopsins. His research contributed towards a deeper understanding of their topologies, structure-functional relations, and mode of action.

Early life

Nazhmutin Abdulaev was born in the Village of Khosrekh (Russian: Хосрех) of Kulinskiy District in the Republic of Dagestan  (North Caucasus,  Russia.)  He was the son of Lak peasant parents - mother Balla Omarova and father Gadzhymagomed Abdulaev. He was the fifth child of the family of 10 children.

Education

Nazhmutin Abdulaev studied nursing at the Medical College of the City of Mahachkala, earning his Bachelor's diploma in 1960. After graduation, he worked as a laboratory technician at the Makhachkala City Blood Transfusion Center. In 1961, he moved to Moscow where he attended the Lomonosov Institute of Fine Chemical Technology. He graduated with a Master’s degree in chemical engineering in 1967.

Career

In 1967, Nazhmutin Abdulaev began his Ph.D studies at the M.M. Shemyakin Institute of Bioorganic Chemistry of the AS USSR (presently, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS.) /7/. He studied peptide and protein chemistry with prof. A.A. Kiryushkin and academician Yu. A. Ovchinnikov /8/ and earned his doctorate in chemistry for establishing the sequence of aspartate aminotransferase in 1973.

He commenced his postdoctoral studies under Ovchinnikov at the laboratory of Protein Chemistry and took command of the group tasked with structure-functional analysis of membrane chromoproteins in 1976.

In 1978, Ovchinnikov and Abdulaev published the sequence and membrane disposition of bacteriorhodopsin [10], the first of true membrane proteins for which a primary structure was achieved [11].

The experience gained from this work was of utmost importance as it demonstrated a value of the combined use of conventional chemical methods and limited proteolysis for structural analysis of hydrophobic membrane proteins in general [11]. Abdulaev applied this experience to studies of other membrane chromoproteins.

In 1982, his group finalized the complete sequence of visual rhodopsin and proposed the topographic model of the protein in the photoreceptor membrane [12]. During the 1980-1990s, Abdulaev published a series of important discoveries as to the structure and function of bacteriorhodopsin and rhodopsin [13-18].

In 1985, in recognition of his substantial accomplishments, Nazhmutin Abdulaev was awarded the highest scientific qualification in Soviet Union, Doctor of Sciences. In 1987, he was appointed a head of the laboratory of Photoreceptor Proteins. In 1988 he published the structures of octopus rhodopsin [19] and M- and L-subunits of Chloroflexus RC [20-21].

After Ovchinnikov’s death in 1988, Abdulaev pursued further research into proteins involved in visual phototransduction /22/ with a particular emphasis on rhodopsin  [23-28].

In 1992, he was appointed Professor of Bioorganic Chemistry. In the same year, he received the Humboldt Research Award for internationally renowned scholars and moved to Frankfurt am Main, Germany. He worked as Visiting Professor at the Max-Plank Institute of Biophysics in the laboratory of Hartmut Michel /29/.

In 1993, Abdulaev moved to the United States, where he worked at the National Institute of Standards and Technology. In collaboration with Kevin Ridge and John Marino, he continued to explore rhodopsin folding, assembly and interaction with G-protein /30/   [31-45]. In 2006, he was appointed Research Professor at the University of Maryland, where he worked until his retirement in 2011.

Nazhmutin Abdulaev served as a Board Member on the International Advisory Committee of the International Conference on Retinal Proteins in 1992, 2002, and 2012[46-48].

In early 2018 he was diagnosed with AML. After 11 months of battling cancer he died at home in Maryland, USA.

Awards and Premiums [1, 49]


 * Awarded the Alexander von Humbolt Research Award (Germany, 1992)
 * Recipient of the USSR and Russia State Prize in Science and Engineering for a cycle of work towards exploration of transmembrane ionic channels (1986)
 * Recipient of the USSR and Russia Federation Order of International Friendship (1986)
 * Recipient of the Shemyakin Prize of the Academy of Sciences of the USSR and Russian Academy of Sciences for publication of work titled “Bioorganic Chemistry of Rhodopsins” (1983)
 * Recipient of the USSR Medal “For Labour Valour” (1981)

External links:

[8] http://www.ibch.ru/en/about/history/personalia/738

[9]

Yu. A. Ovchinnikov, C.A.Egorov, N.A. Aldanova, M.Yu. Feigina, V.M. Lipkin, N.G. Abdulaev,  E.V.Grishin, A.P. Kiselev, N.N. Modyanov, A.E. Braunstein, O.L. Polyanovsky, V.V.Nosikov (1973) The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart. FEBS Lett 29 (1), 31–34  

PMID: 11946901

DOI: 10.1016/0014-5793(73)80008-0

https://doi.org/10.1016/0014-5793(73)80008-0

[10]

Ovchinnikov, Yu.A., Abdulaev, N.G., Feigina, M.Yu., Kiselev, A.V., Lobanov, N.A., and Nazimov, I.V. (1978) The amino acid sequence of bacteriorhodopsin. Bioorg. Khim. 4, 1573-1574. Russian)

http://rjbc.ru/arc/4/11/1573-1574.pdf

[11]

Ovchinnikov, Yu.A., Abdulaev, N.G., Feigina, M.Yu., Kiselev, A.V., Lobanov, N.A. (1979) The structural basis of the functioning of bacteriorhodopsin: an overview. FEBS let. 100, 219-224

PMID: 378693

DOI: 10.1016/0014-5793(79)80338-5

https://doi.org/10.1016/0014-5793(79)80338-5

[12]

Ovchinnikov, Yu. A., Abdulaev, N. G., Feigina, M. Yu., Artamonov, I. D., Zolotarev, A. S., Kostina, M. B., Bogachuk, A. S., Miroshnikov, A. I, Martynov, V. I,  Kudelin, A. B.(1982) The complete amino acid sequence of visual rhodopsin. Bioorg. Chem. 8 (10):1424-1427. Russian

http://www.rjbc.ru/arc/8/10/1424-1427.pdf

[13]

Abdulaev, N. G., Feigina, M. Yu., Kiselev, A. V., Ovchinnikov, Yu. A., Drachev, L. A., Kaulen, A. D., Khitrina, L. V., and Skulachev V. P.(1978) Products of limited proteolysis of bacteriorhodopsin generate a membrane potential. FEBS Lett. 90:190–194.

PMID: 668882

DOI: 10.1016/0014-5793(78)80366-4

https://doi.org/10.1016/0014-5793(78)80366-4

[14]

Yu.A. Ovchinnikov,  N.G. Abdulaev,  R.G. Vasilov,  I.Yu. Vturina, A.B. Kuryatov,  A.V. Kiselev (1985) The antigenic structure and topography of bacteriorhodopsin in purple membranes as determined by interaction with monoclonal antibodies. FEBS Lett 179 (2), 343-350

DOI: 10.1016/0014-5793(85)80548-2

https://doi.org/10.1016/0014-5793(85)80548-2

[15]

Ovchinnikov Y.A., Abdulaev N.G. (1985) Bacteriorhodopsin and Rhodopsin Structure and Function. In: Martonosi A.N. (eds) The Enzymes of Biological Membranes. Springer, Boston, MA

DOI: 10.1007/978-1-4684-4604-3_16

https://doi.org/10.1007/978-1-4684-4604-3_16

[16]

N. G. Abdulaev, N. A. Dencher, A. E. Dergachev, A. Fahr, A. V. Kiselev (1983) The chromophore retinal in bacteriorhodopsin does not change its attachment site, lysine 216, during proton translocation and light-dark adaptation. European Biophysics Journal 10(4):211-227

Online ISSN: 1432-1017

DOI: 10.1007/BF00535550

https://doi.org/10.1007/BF00535550

[17]

Sigrist H, Allegrini PR, Stauffer K, Schaller J, Abdulaev NG, Rickli EE, Zahler P (1984). ''Group-directed modification of bacteriorhodopsin by arylisothiocyanates. Labeling, identification of the binding site and topology''.J Mol Biol 173 (1), 93–108

PMID: 6321744

DOI: 10.1016/0022-2836(84)90405-4

https://doi.org/10.1016/0022-2836(84)90405-4

[18]

Yu.A. Ovchinnikov, N.G. Abdulaev, A.S. Bogachuk (1988) Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS Lett 230 (1,2), 1–5

PMID: 3350146

DOI: 10.1016/0014-5793(88)80628-8

https://doi.org/10.1016/0014-5793(88)80628-8

[19]

Ovchinnikov YuA, Abdulaev NG, Zolotarev AS, Artamonov ID, Bespalov IA, Dergachev AE, Tsuda M. (1988) ''Octopus rhodopsin. Amino acid sequence deduced from cDNA.'' FEBS Lett. 232(1):69-72.

PMID: 3366250

DOI: 10.1016/0014-5793(88)80388-0

https://doi.org/10.1016/0014-5793(88)80388-0

[20]

Ovchinnikov YuA, Abdulaev NG, Shmuckler BE, Zargarov AA, Kutuzov MA, Telezhinskaya IN, Levina NB, Zolotarev AS. (1988)''Photosynthetic reaction centre of Chloroflexus aurantiacus. Primary structure of M-subunit''. FEBS Lett. 232(2):364-8.

PMID: 3288502

DOI: 10.1016/0014-5793(88)80770-1

https://doi.org/10.1016/0014-5793(88)80770-1

[21]

Ovchinnikov YuA, Abdulaev NG, Zolotarev AS, Shmukler BE, Zargarov AA, Kutuzov MA, Telezhinskaya IN, Levina NB. (1988) ''Photosynthetic reaction centre of Chloroflexus aurantiacus. I. Primary structure of L-subunit.'' FEBS Lett. Apr 11;231(1):237-42.

DOI: 10.1016/0014-5793(88)80739-7

https://doi.org/10.1016/0014-5793(88)80739-7

/22/ Internal WIKI link

https://en.wikipedia.org/wiki/Visual_phototransduction

[23]

Dergachev AE, Artamov ID, Bespalov IA, Zolotarev AS, Abdulaev NG. (1989) Octopus rhodopsin: unusual C-terminal fragment. J Protein Chem. 8(3):382-4.

Online ISSN1573-4943

DOI: 10.1007/BF01674290

https://doi.org/10.1007/BF01674290

[24]

Yurkova EV, Demin VV, Abdulaev NG. (1990) Crystallization of membrane proteins: bovine rhodopsin. Biomed Sci.1(6):585-90.

PMID: 2132942

https://www.ncbi.nlm.nih.gov/pubmed/2132942

[25]

Kutuzov MA, Shmukler BE, Suslov ON, Dergachev AE, Zargarov AA, Abdulaev NG. (1991) P26-calcium binding protein from bovine retinal photoreceptor cells. FEBS Lett. 293(1-2):21-4.

PMID: 1959664

DOI: 10.1016/0014-5793(91)81143-V

https://doi.org/10.1016/0014-5793(91)81143-V

[26]

Kutuzov MA, Shmukler BE, Suslov ON, Zargarov AA, Abdulaev NG. (1992) p26--a calcium binding protein from photoreceptor cells in the bovine retina: primary structure and expression in E. coli. Bioorg Khim. 18(5):623-634. Russian

PMID:1417990

http://rjbc.ru/arc/18/5/0623-0634.pdf

[27]

Gaidarov IO, Suslov ON, Abdulaev NG. (1993) ''Enzymes of the cyclic GMP metabolism in bovine retina. I. Cloning and expression of the gene for guanylate kinase.'' FEBS Lett. 335(1):81-4.

PMID: 8243671

DOI: 10.1016/0014-5793(93)80444-Y

https://doi.org/10.1016/0014-5793(93)80444-Y

[28]

Gaĭdarov IO, Suslov ON, Ovchinnikova TV, Abdulaev NG. (1994) Guanylate kinase from bovine retina: isolation, primarystructure, and expression in E. coli. Bioorg Khim. 20(4):367-381. Russian

PMID: 7911663

http://rjbc.ru/arc/20/4/0367-0381.pdf

Internal WIKI links:

/29/  https://en.wikipedia.org/wiki/Hartmut_Michel

/30/  https://en.wikipedia.org/wiki/G_protein

[31]

Ridge KD, Lee SS, Abdulaev NG. (1996) Examining rhodopsin folding and assembly through expression of polypeptide fragments. J Biol Chem. 271(13):7860-7.

PMID: 8631831

DOI: 10.1074/jbc.271.13.7860

[32]

Abdulaev NG, Karaschuk GN, Ladner JE, Kakuev DL, Yakhyaev AV, Tordova M, Gaidarov IO, Popov VI, Fujiwara JH, Chinchilla D, Eisenstein E, Gilliland GL, Ridge KD. (1998) Nucleoside diphosphate kinase from bovine retina: purification, subcellular localization, molecular cloning, and three-dimensional structure. Biochemistry. Oct 6;37(40):13958-67.

PMID: 9760230

DOI: 10.1021/bi980853s

[33]

Abdulaev NG, Ridge KD. (1998) Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin. Proc Natl Acad Sci U S A. 95(22):12854-9.

PMID: 9789004

DOI: 10.1073/pnas.95.22.12854

[34]

Ladner JE, Abdulaev NG, Kakuev DL, Tordová M, Ridge KD, Gilliland GL. (1999) The three-dimensional structures of two isoforms of nucleoside diphosphate kinase from bovine retina. Acta Crystallogr D Biol Crystallogr. Jun; 55(Pt 6):1127-35.

PMID: 10329774

DOI: 10.1107/s0907444999002528

[35]

Ridge KD, Ngo T, Lee SS, Abdulaev NG. (1999) ''Folding and assembly in rhodopsin. Effect of    mutations in the sixth transmembrane helix on the conformation of the third cytoplasmic loop.'' J Biol Chem. Jul 23;274(30):21437-42.

PMID: 10409707

DOI: 10.1074/jbc.274.30.21437

[36]

Abdulaev NG, Kakuev DL, Ridge KD. (2000) Bovine retinal nucleoside diphosphate kinase: biochemistry and molecular cloning.Methods Enzymol. 316:87-100.

PMID: 10800670

DOI: 10.1016/s0076-6879(00)16718-7

[37]

Ridge KD, Abdulaev NG. (2000) Folding and assembly of rhodopsin from expressed fragments. Methods Enzymol. 315:59-70.

PMID: 10736693

DOI: 10.1016/s0076-6879(00)15834-3

[38]

Abdulaev NG, Strassmaier TT, Ngo T, Chen R, Luecke H, Oprian DD, Ridge KD. (2002) Grafting segments from the extracellular surface of CCR5 onto a bacteriorhodopsin transmembrane scaffold confers HIV-1 coreceptor activity.Structure. Apr;10(4):515-25.

PMID: 11937056

DOI: 10.1016/s0969-2126(02)00752-9

[39]

Abdulaev NG. (2003) Building a stage for interhelical play in rhodopsin. Trends Biochem Sci. Aug;28(8):399-402. Review.

PMID: 12932725

DOI: 10.1016/S0968-0004(03)00164-6

[40]

Brabazon DM, Abdulaev NG, Marino JP, Ridge KD (2003) Evidence for structural changes in carboxyl-terminal peptides of transducin alpha-subunit upon binding a soluble mimic of light-activated rhodopsin. Biochemistry. Jan 21;42(2):302-11.

PMID:12525157

DOI:10.1021/bi0268899

[41]

Abdulaev NG, Ngo, T., Zhang C, Dinh A, Brabazon, D.M., Ridge, K.D., Marino, J.P. (2005) Heterometric G protein alpha subunit adopts a “preactivated conformation” when associated with betagamma subunits. J.Biol. Chem. 280 (45) 38071-31080.

PMID: 16129667

DOI: 10.1074/jbc.M505259200

[42]

Ridge KD, Abdulaev NG, Zhang C, Ngo T, Brabazon DM, Marino JP. (2006) Conformational changes associated with receptor-stimulated guanine nucleotide exchange in a heterotrimeric G-protein alpha-subunit: NMR analysis of GTP gamma S-bound states.J Biol Chem. Mar 17;281(11):7635-48.

PMID: 16407225

DOI: 10.1074/jbc.M509851200

[43]

Ridge KD, Marino JP, Ngo T, Ramon E, Brabazon DM, Abdulaev NG. (2006) NMR analysis of rhodopsin-transducin interactions.Vision Res. Dec;46(27):4482-92.

PMID: 16979691

DOI: 10.1016/j.visres.2006.07.024

[44]

Abdulaev NG, Ngo T, Ramon E, Brabazon DM, Marino JP, Ridge KD. (2006) The receptor-bound "empty pocket" state of the heterotrimeric G-protein alpha-subunit is conformationally dynamic. Biochemistry. Oct 31;45(43):12986-97.

PMID: 17059215

DOI: 10.1021/bi061088h

[45]

Abdulaev NG, Mao X, Ramon E, Ngo T, Mysliwy J, Marino JP, Ridge KD. (2009) Designing point mutants to detect structural coupling in a heterotrimeric G protein alpha-subunit by NMR spectroscopy. Photochem Photobiol. Mar-Apr;85(2):431-6.

PMID:19222798

DOI:10.1111/j.1751-1097.2008.00522.x

[46]

https://books.google.com/books?id=3PY8fgVvS0MC&pg=PR6&lpg=PR6&dq=Conference+on+Retinal+Proteins,+abdulaev&source=bl&ots=yRwD4FPIdc&sig=ACfU3U2h-YwdJbCCTk9xiYPhlCJqkuJ2Hg&hl=en&sa=X&ved=2ahUKEwix1OeusM_kAhVLuZ4KHfGbAzwQ6AEwEXoECAcQAQ#v=onepage&q=Conference%20on%20Retinal%20Proteins%2C%20abdulaev&f=false

[47]  https://apps.dtic.mil/dtic/tr/fulltext/u2/a417042.pdf

[48]  https://indico.psi.ch/event/1387/page/73-advisory-committee

[49]  http://www.ibch.ru/en/about/history/honors/1543