Photosynthesis Research

, Volume 129, Issue 1, pp 1–12 | Cite as

Remembering David B. Knaff (1941–2016)

  • Richard MalkinEmail author


David Knaff began his scientific career in the Department of Cell Physiology at the University of California, Berkeley. At Berkeley, he worked on chloroplast electron carriers such as the cytochromes and plastocyanin and applied redox potentiometry to characterize these carriers in situ. He moved to Texas Tech University where he made major contributions in the study of ferredoxin-mediated reactions with chloroplast enzymes, most notably nitrite reductase.


Chloroplasts Ferredoxin Nitrite Reductase Electron Transfer Oxidation–reduction potentials 



I would like to thank all David’s friends and colleagues who contributed to this Tribute. Their timely response to my requests made my task much easier. In some cases, I did some minor editing of their contributions, and I hope they will forgive me for taking this liberty.


  1. Aparicio PJ, Knaff DB, Malkin R (1975) The role of an iron-sulfur center and siroheme in spinach nitrite reductase. Arch Biochem Biopys 169:102–107CrossRefGoogle Scholar
  2. Hirasawa M, Shaw RW, Palmer G, Knaff DB (1987) Prosthetic group content and ligand-binding properties of spinach nitrite reductase. J Biol Chem 262:12428–12433PubMedGoogle Scholar
  3. Hirasawa M, Tripathy JN, Somasundaram R, Johnson MK, Bhalla M, Allen J, Knaff DB (2009) The interaction of spinach nitrite reductase with ferredoxin: a site-directed mutation study. Mol Plant 2:407–415CrossRefPubMedPubMedCentralGoogle Scholar
  4. Hirasawa M, Tripathy JN, Sommer F, Somasundaram R, Chung J, Nestander M, Kruthiventi M, Zabet-Moghaddam M, Johnson MK, Merchant S, Allen JP, Knaff DB (2010) Enzymatic properties of the ferredoxin-dependent nitrite reductase from Chlamydomonas reinhardtii. Evidence for hydroxylamine as a late intermediate in ammonia production. Photosynth Res 103:67–77CrossRefPubMedGoogle Scholar
  5. Knaff DB (1993) The cytochrome bc 1 complexes of photosynthetic purple bacteria. Photosynth Res 35:117–133CrossRefPubMedGoogle Scholar
  6. Knaff DB, Arnon DI (1969a) Light-induced oxidation of a chloroplast b-type cytochrome at −189 °C. Proc Natl Acad Sci 63:956–962CrossRefPubMedPubMedCentralGoogle Scholar
  7. Knaff DB, Arnon DI (1969b) Spectral evidence for a new photoreactive component of the oxygen-evolving system in photosynthesis. Proc Natl Acad Sci 63:963–969CrossRefPubMedPubMedCentralGoogle Scholar
  8. Knaff DB, Malkin R (1976) Iron-sulfur proteins of the green photosynthetic bacterium Chlorobium. Biochim Biophys Acta 430:244–252CrossRefPubMedGoogle Scholar
  9. Malkin R, Knaff DB, Bearden A (1973) The oxidation-reduction potential of membrane-bound chloroplast plastocyanin and cytochrome f. Biochim Biophys Acta 305:675–678CrossRefPubMedGoogle Scholar
  10. Setif P, Hirasawa M, Cassan N, Lagoutte B, Tripathy JN, Knaff DB (2009) New insights into the catalytic cycle of plant nitrite reductase. Electron transfer kinetics and charge storage. Biochemistry 48:2828–2838CrossRefPubMedGoogle Scholar
  11. Stoller M, Malkin R, Knaff DB (1977) Oxidation-reduction properties of photosynthetic nitrite reductase. FEBS Lett 81:271–274CrossRefGoogle Scholar
  12. Swamy U, Wang M, Tripathy JN, Kim S, Hirasawa M, Knaff DB, Allen J (2005) Structure of spinach nitrite reductase: implications for multi-electron reactions by the iron–sulfur: siroheme cofactor. Biochemistry 44:16054–16063CrossRefPubMedGoogle Scholar
  13. Wynn RM, Redlinger TE, Foster JM, Blankenship RE, Fuller RC, Shaw RW, Knaff DB (1987) Electron transport chains of phototrophically and chemotrophically grown Chloroflexus aurantiacus. Biochim Biophys Acta 891:216–226CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  1. 1.Department of Plant and Microbial BiologyUniversity of CaliforniaBerkeleyUSA

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