H. Haaker

2.2k total citations
57 papers, 1.7k citations indexed

About

H. Haaker is a scholar working on Renewable Energy, Sustainability and the Environment, Molecular Biology and Materials Chemistry. According to data from OpenAlex, H. Haaker has authored 57 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Renewable Energy, Sustainability and the Environment, 24 papers in Molecular Biology and 12 papers in Materials Chemistry. Recurrent topics in H. Haaker's work include Metalloenzymes and iron-sulfur proteins (39 papers), Electrocatalysts for Energy Conversion (11 papers) and Hydrogen Storage and Materials (10 papers). H. Haaker is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (39 papers), Electrocatalysts for Energy Conversion (11 papers) and Hydrogen Storage and Materials (10 papers). H. Haaker collaborates with scholars based in Netherlands, United States and United Kingdom. H. Haaker's co-authors include C. Veeger, Hans Wassink, Wilfred R. Hagen, Colja Laane, Robert R. Eady, Wil N. Konings, W Krone, E. Racker, Antonio J. Pierik and Pedro J. Silva and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and PLANT PHYSIOLOGY.

In The Last Decade

H. Haaker

57 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
H. Haaker Netherlands 25 940 617 319 271 241 57 1.7k
R. Premakumar United States 20 575 0.6× 436 0.7× 462 1.4× 191 0.7× 121 0.5× 38 1.7k
Robert L. Robson United Kingdom 19 503 0.5× 568 0.9× 228 0.7× 101 0.4× 288 1.2× 26 1.4k
Francis Blasco France 25 991 1.1× 946 1.5× 147 0.5× 98 0.4× 443 1.8× 32 1.9k
David H. Boxer United Kingdom 31 1.5k 1.6× 1.6k 2.6× 239 0.7× 141 0.5× 280 1.2× 74 3.1k
William A. Bulen United States 17 554 0.6× 492 0.8× 375 1.2× 182 0.7× 86 0.4× 24 1.5k
Marcel Asso France 24 780 0.8× 655 1.1× 154 0.5× 79 0.3× 414 1.7× 57 1.6k
Bruno Guigliarelli France 34 2.2k 2.3× 753 1.2× 120 0.4× 234 0.9× 645 2.7× 62 3.0k
Luis M. Rubio Spain 29 1.7k 1.8× 781 1.3× 655 2.1× 620 2.3× 243 1.0× 72 2.7k
Yves Jouanneau France 31 667 0.7× 1.1k 1.8× 228 0.7× 111 0.4× 332 1.4× 66 2.4k
Túlio Morgan United States 22 550 0.6× 398 0.6× 114 0.4× 119 0.4× 291 1.2× 59 1.2k

Countries citing papers authored by H. Haaker

Since Specialization
Citations

This map shows the geographic impact of H. Haaker'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 H. Haaker with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites H. Haaker more than expected).

Fields of papers citing papers by H. Haaker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by H. Haaker. 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 H. Haaker. The network helps show where H. Haaker may publish in the future.

Co-authorship network of co-authors of H. Haaker

This figure shows the co-authorship network connecting the top 25 collaborators of H. Haaker. A scholar is included among the top collaborators of H. Haaker 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 H. Haaker. H. Haaker 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.
Hagen, Wilfred R., Pedro J. Silva, Maria Amélia Amorim, et al.. (2000). Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. JBIC Journal of Biological Inorganic Chemistry. 5(4). 527–534. 52 indexed citations
2.
Spee, Johan H., Alexander F. Arendsen, Hans Wassink, et al.. (1998). Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase. FEBS Letters. 432(1-2). 55–58. 23 indexed citations
3.
Wassink, Hans, et al.. (1996). Pre-steady-state Kinetics of Nitrogenase from Azotobacter vinelandii. Journal of Biological Chemistry. 271(47). 29632–29636. 15 indexed citations
4.
Wassink, Hans, et al.. (1996). Formation and characterization of a transition state complex of Azotobacter vinelandii nitrogenase. FEBS Letters. 380(3). 233–236. 54 indexed citations
5.
Haaker, H., et al.. (1995). Properties of the Peribacteroid Membrane ATPase of Pea Root Nodules and Its Effect on the Nitrogenase Activity. PLANT PHYSIOLOGY. 108(3). 1227–1232. 24 indexed citations
6.
Wassink, Hans, et al.. (1994). Pre‐Steady‐State MgATP‐Dependent Proton Production and Electron Transfer by Nitrogenase from Azotobacter vinelandii. European Journal of Biochemistry. 225(3). 881–890. 7 indexed citations
7.
Pierik, Antonio J., Hans Wassink, H. Haaker, & Wilfred R. Hagen. (1993). Redox properties and EPR spectroscopy of the P clusters of Azotobacter vinelandii MoFe protein. European Journal of Biochemistry. 212(1). 51–61. 100 indexed citations
8.
Wassink, Hans, et al.. (1992). A reinvestigation of the pre‐steady‐state ATPase activity of the nitrogenase from Azotobacter vinelandii. European Journal of Biochemistry. 208(2). 289–294. 12 indexed citations
9.
Haaker, H., et al.. (1992). Temperature effects on the MgATP‐induced electron transfer between the nitrogenase proteins from Azotobacter vinelandii. European Journal of Biochemistry. 208(2). 295–299. 9 indexed citations
10.
Hagen, Wilfred R., Antonio J. Pierik, Ronnie B. G. WOLBERT, et al.. (1991). Superclusters with superspins in iron-sulfur redox enzymes.. BioFactors. 3. 144–144. 2 indexed citations
11.
Haaker, H., et al.. (1991). Glutamate Oxaloacetate Transaminase in Pea Root Nodules. PLANT PHYSIOLOGY. 95(3). 740–747. 47 indexed citations
12.
Haaker, H., et al.. (1988). Identification of cytoplasmic nodule‐associated forms of malate dehydrogenase involved in the symbiosis between Rhizobium leguminosarum and Pisum sativum. European Journal of Biochemistry. 171(3). 515–522. 22 indexed citations
13.
CORDEWENER, Jan, et al.. (1988). The role of MgATP hydrolysis in nitrogenase catalysis. European Journal of Biochemistry. 172(3). 739–745. 9 indexed citations
14.
Hagen, Wilfred R., Hans Wassink, Robert R. Eady, B. E. Smith, & H. Haaker. (1987). S=7/2 EPR of the P-clusters in thionine oxidized MoFe-proteins of nitrogenase.. Recueil des Travaux Chimiques des Pays-Bas. 106. 229–229. 1 indexed citations
15.
Hagen, Wilfred R., Hans Wassink, Robert R. Eady, Barry E. Smith, & H. Haaker. (1987). Quantitative EPR of an S= 7/2 system in thionine‐oxidized MoFe proteins of nitrogenase. European Journal of Biochemistry. 169(3). 457–465. 73 indexed citations
16.
Dunham, William, et al.. (1985). The importance of quantitative Mossbauer spectroscopy of MoFe-protein from Azotobacter vinelandii. European Journal of Biochemistry. 146(3). 497–501. 14 indexed citations
17.
Haaker, H., et al.. (1983). Fully Active Fe‐Protein of the Nitrogenase from Azotobacter vinelandii Contains at least Eight Iron Atoms and Eight Sulphide Atoms per Molecule. European Journal of Biochemistry. 133(1). 71–76. 17 indexed citations
18.
Haaker, H., et al.. (1982). Short‐Term Regulation of the Nitrogenase Activity in Rhodopseudomonas sphaeroides. European Journal of Biochemistry. 127(3). 639–646. 37 indexed citations
19.
Laane, Colja, W Krone, Wil N. Konings, H. Haaker, & C. Veeger. (1979). The involvement of the membrane potential in nitrogen fixation by bacteroids of Rhizobium leguminosarum. FEBS Letters. 103(2). 328–332. 34 indexed citations
20.
Haaker, H. & E. Racker. (1979). Purification and reconstitution of the Ca2+-ATPase from plasma membrane of pig erythrocytes.. Journal of Biological Chemistry. 254(14). 6598–6602. 54 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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