Igor D. Petrik

1.8k total citations · 1 hit paper
20 papers, 1.4k citations indexed

About

Igor D. Petrik is a scholar working on Inorganic Chemistry, Molecular Biology and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, Igor D. Petrik has authored 20 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Inorganic Chemistry, 10 papers in Molecular Biology and 7 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Igor D. Petrik's work include Metal-Catalyzed Oxygenation Mechanisms (12 papers), Photosynthetic Processes and Mechanisms (7 papers) and Metalloenzymes and iron-sulfur proteins (7 papers). Igor D. Petrik is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (12 papers), Photosynthetic Processes and Mechanisms (7 papers) and Metalloenzymes and iron-sulfur proteins (7 papers). Igor D. Petrik collaborates with scholars based in United States, China and Sweden. Igor D. Petrik's co-authors include Yi Lu, Parisa Hosseinzadeh, Yang Yu, Saumen Chakraborty, Jing Liu, Shiliang Tian, Jing Liu, Howard Robinson, Ambika Bhagi‐Damodaran and Mark J. Nilges and has published in prestigious journals such as Science, Chemical Reviews and Journal of the American Chemical Society.

In The Last Decade

Igor D. Petrik

20 papers receiving 1.4k citations

Hit Papers

Metalloproteins Containing Cytochrome, Iron–Sulfur, or Co... 2014 2026 2018 2022 2014 200 400 600

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Igor D. Petrik United States 14 621 434 426 324 232 20 1.4k
Parisa Hosseinzadeh United States 20 956 1.5× 453 1.0× 422 1.0× 325 1.0× 218 0.9× 36 1.8k
Saumen Chakraborty United States 17 668 1.1× 371 0.9× 485 1.1× 692 2.1× 256 1.1× 41 1.8k
Changjian Feng United States 24 581 0.9× 316 0.7× 515 1.2× 214 0.7× 292 1.3× 100 1.8k
A. Andrew Pacheco United States 21 444 0.7× 360 0.8× 610 1.4× 207 0.6× 180 0.8× 40 1.4k
Natasha Yeung United States 12 717 1.2× 372 0.9× 282 0.7× 296 0.9× 145 0.6× 12 1.3k
Nicholas Marshall United States 22 864 1.4× 517 1.2× 382 0.9× 441 1.4× 506 2.2× 38 2.1k
Takamitsu Kohzuma Japan 24 903 1.5× 561 1.3× 372 0.9× 358 1.1× 174 0.8× 95 1.7k
Yi-Gui Gao United States 11 498 0.8× 274 0.6× 181 0.4× 344 1.1× 109 0.5× 12 1.0k
Akira Onoda Japan 27 814 1.3× 409 0.9× 464 1.1× 555 1.7× 306 1.3× 98 2.1k
Shiliang Tian United States 18 744 1.2× 479 1.1× 624 1.5× 709 2.2× 330 1.4× 35 2.6k

Countries citing papers authored by Igor D. Petrik

Since Specialization
Citations

This map shows the geographic impact of Igor D. Petrik's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Igor D. Petrik with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Igor D. Petrik more than expected).

Fields of papers citing papers by Igor D. Petrik

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Igor D. Petrik. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Igor D. Petrik. The network helps show where Igor D. Petrik may publish in the future.

Co-authorship network of co-authors of Igor D. Petrik

This figure shows the co-authorship network connecting the top 25 collaborators of Igor D. Petrik. A scholar is included among the top collaborators of Igor D. Petrik based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Igor D. Petrik. Igor D. Petrik is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Petrik, Igor D., Roman Davydov, Braddock A. Sandoval, et al.. (2021). An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity by Tuning the Hydrogen-Bonding Network. Biochemistry. 60(4). 346–355. 6 indexed citations
2.
Mirts, Evan N., Igor D. Petrik, Parisa Hosseinzadeh, Mark J. Nilges, & Yi Lu. (2018). A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme. Science. 361(6407). 1098–1101. 118 indexed citations
3.
Reed, Julian H., Qianhong Zhu, Saumen Chakraborty, et al.. (2017). Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism. Journal of the American Chemical Society. 139(35). 12209–12218. 32 indexed citations
5.
Powis, Zöe, Igor D. Petrik, Julie S. Cohen, et al.. (2017). De novo variants in KLF7 are a potential novel cause of developmental delay/intellectual disability, neuromuscular and psychiatric symptoms. Clinical Genetics. 93(5). 1030–1038. 12 indexed citations
6.
Bhagi‐Damodaran, Ambika, Igor D. Petrik, & Yi Lu. (2016). Using Biosynthetic Models of Heme‐Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities. Israel Journal of Chemistry. 56(9-10). 773–790. 26 indexed citations
7.
Bhagi‐Damodaran, Ambika, Parisa Hosseinzadeh, Evan N. Mirts, et al.. (2016). Design of Heteronuclear Metalloenzymes. Methods in enzymology on CD-ROM/Methods in enzymology. 580. 501–537. 5 indexed citations
8.
Yu, Yang, Igor D. Petrik, Kelly N. Chacón, et al.. (2016). Effect of circular permutation on the structure and function of type 1 blue copper center in azurin. Protein Science. 26(2). 218–226. 13 indexed citations
9.
Yu, Yang, Chang Cui, Xiaohong Liu, et al.. (2015). A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme. Journal of the American Chemical Society. 137(36). 11570–11573. 71 indexed citations
10.
Petrik, Igor D., Roman Davydov, Matthew O. Ross, et al.. (2015). Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin. Journal of the American Chemical Society. 138(4). 1134–1137. 27 indexed citations
11.
Chakraborty, Saumen, Julian H. Reed, J. Timothy Sage, et al.. (2015). Recent Advances in Biosynthetic Modeling of Nitric Oxide Reductases and Insights Gained from Nuclear Resonance Vibrational and Other Spectroscopic Studies. Inorganic Chemistry. 54(19). 9317–9329. 20 indexed citations
12.
Petrik, Igor D., et al.. (2014). Výskyt margaritu a pumpellyitu (Al) v metamorfovaných horninách Malej Magury: Stanovenie P-T podmienok metamorfizmu a kryštalizácie asociujúcich granitoidov. 6(2). 169–178. 1 indexed citations
13.
Chakraborty, Saumen, Julian H. Reed, Matthew O. Ross, et al.. (2014). Spectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide Reductase. Angewandte Chemie International Edition. 53(9). 2417–2421. 34 indexed citations
14.
Petrik, Igor D., Jing Liu, & Yi Lu. (2014). Metalloenzyme design and engineering through strategic modifications of native protein scaffolds. Current Opinion in Chemical Biology. 19. 67–75. 88 indexed citations
15.
Chakraborty, Saumen, Julian H. Reed, Matthew O. Ross, et al.. (2014). Spectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide Reductase. Angewandte Chemie. 126(9). 2449–2453. 10 indexed citations
16.
Liu, Jing, Saumen Chakraborty, Parisa Hosseinzadeh, et al.. (2014). Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers. Chemical Reviews. 114(8). 4366–4469. 687 indexed citations breakdown →
17.
Bhagi‐Damodaran, Ambika, Igor D. Petrik, Nicholas Marshall, Howard Robinson, & Yi Lu. (2014). Systematic Tuning of Heme Redox Potentials and Its Effects on O2 Reduction Rates in a Designed Oxidase in Myoglobin. Journal of the American Chemical Society. 136(34). 11882–11885. 79 indexed citations
18.
Miner, Kyle D., Arnab Mukherjee, Yi‐Gui Gao, et al.. (2012). A Designed Functional Metalloenzyme that Reduces O2 to H2O with Over One Thousand Turnovers. Angewandte Chemie International Edition. 51(23). 5589–5592. 98 indexed citations
19.
Miner, Kyle D., Arnab Mukherjee, Yi‐Gui Gao, et al.. (2012). A Designed Functional Metalloenzyme that Reduces O2 to H2O with Over One Thousand Turnovers. Angewandte Chemie. 124(23). 5687–5690. 14 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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