Source: GORDON RESEARCH CONFERENCES, INC submitted to NRP
2004 NITROGEN FIXATION GORDON CONFERENCE
Sponsoring Institution
National Institute of Food and Agriculture
Project Status
COMPLETE
Funding Source
NRI COMPETITIVE GRANT
Reporting Frequency
Annual
Accession No.
0200941
Grant No.
2004-35318-14950
Cumulative Award Amt.
(N/A)
Proposal No.
2004-02996
Multistate No.
(N/A)
Project Start Date
Sep 1, 2004
Project End Date
Aug 31, 2005
Grant Year
2004
Program Code
[54.3]- (N/A)
Recipient Organization
GORDON RESEARCH CONFERENCES, INC
512 LIBERTY LN
WEST KINGSTON,RI 02892-1502
Performing Department
(N/A)
Non Technical Summary
Nitrogen is an element that is essential for all living organisms, and despite the abundance of dinitrogen gas in the atmosphere, the availability of combined forms is typically limiting for agricultural systems, and often for natural ecosystems. Nitrogen fixation is the conversion of nitrogen gas to ammonia and in biological systems is catalyzed by a complex metal-containing enzyme termed nitrogenase. In countries with intensive agriculture, increased concerns for run-off of fertilizer nitrogen are leading to limits on fertilizer application and a return to emphasis on biological nitrogen fixation. Thus nitrogen fixation research could have significant agronomic, economic, and environmental implications. A detailed fundamental understanding of the workings of nitrogenase will contribute greatly to evaluating potential avenues of better harnessing or mimicking this process for more efficient production of fixed nitrogen. The nitrogenase enzyme itself is a fascinating complex metal-containing enzyme. The enzyme belongs to a class of metal-containing enzymes that possess biological bridged metal assemblies which also includes certain hydrogenases, acetyl coenzyme A synthase, and sulfite reductase. The common characteristics of these enzymes is that they all contain FeS clusters with a [4Fe-4S] cubane or some derivative thereof bridged to another metal containing group via sulfides or thiolates. Thus, nitrogenase is a fascinating model system for the study of metal-cluster mediated catalysis and electronic structure.
Animal Health Component
(N/A)
Research Effort Categories
Basic
100%
Applied
(N/A)
Developmental
(N/A)
Classification

Knowledge Area (KA)Subject of Investigation (SOI)Field of Science (FOS)Percent
2062499100075%
2062499104025%
Knowledge Area
206 - Basic Plant Biology;

Subject Of Investigation
2499 - Plant research, general;

Field Of Science
1040 - Molecular biology; 1000 - Biochemistry and biophysics;
Goals / Objectives
Conduct a scientific meeting on the topic of nitrogen fixation. The meeting will focus on structure/function relationships in the complex iron-sulfur cluster-containing enzyme nitrogenase. Nitrogenase catalyzes the reduction of atmospheric gas to ammonia and thus the detailed studies on the mechanism of this interesting enzyme could potentially have a large impact on global plant productivity and nutrition. The objectives of the meeting will be to disseminate the latest experimental results, foster the involvement and research goals of new investigators, and stimulate scientific collaborations and cooperative efforts within the field.
Project Methods
The approach or organization for the meeting adheres to the general format for the Gordon Research Conferences consisting of morning and evening meetings, afternoon and evening poster sessions, and free unstructured afternoon time for informal scientific discussions. The schedule represents a mix of established investigators and young investigators. The meeting features an prestigious Alexander Cruickshank named lectureship to Professor Douglas C. Rees of the California Institute of Technology.

Progress 09/01/04 to 08/31/05

Outputs
The 10th Gordon Research Conference on nitrogen fixation was held at Colby-Sawyer College on June 20-25, 2004 Colby-Sawyer College New London, NH. The meeting began with a tribute to the numerous contributions Robert Burris of the University of Wisconsin by Professor Paul Ludden of University of California at Berkeley. Professor Burris is one of the pioneers in the area of nitrogenase biochemistry and laid the groundwork for numerous investigators in attendance at the meeting. This lecture was followed by the Alexander Cruikshank lecture in chemistry given by Douglas C. Rees of the California Institute of Technology. This Cruikshank Lectureship recognizes profound achievements of a few speakers in the topics represented in the Gordon Research Conferences. Professor Rees provided an excellent lecture on his personal contributions to the field in the context of the structural basis for nitrogenase function. These lectures set the stage for an excellent meeting which represented a mix of established investigators and new investigators. Approximately seventy attendees were exposed to approximately thirsty lectures that covered the topics of nitrogenase biochemistry, inorganic synthetic models, theoretical chemistry, and the broader areas of iron-sulfur cluster biosynthesis and related iron-sulfur enzymes. The latter aspects of the conference were very successful and it was decided at the conference to broaden the scope of the meeting and change its name to the Gordon Research Conference on Iron-Sulfur Enzymes. The meeting will remain to have as a major focus nitrogen fixation but the new format will allow significant contributions from researchers investigating the related hydrogenase, carbon monoxide dehydrogenase / acetyl coenzyme A synthase, radical SAM enzymes, and iron-sulfur cluster biosynthesis. The meeting will now facilitate nitrogen fixation research by providing a forum for the interactions of nitrogenase researchers with investigators in these other exciting areas of iron-sulfur cluster biochemistry. The closing lecture of the meeting was given by Roger Thorneley of the John Innes Center in Norwich, UK. Professor Thorneley has been a member of the Royal Society of Chemistry for approximately 20 years and he and his colleagues at the JIC have made numerous fundamental contributions in the area of nitrogenase biochemistry. Professor Thorneley is soon to retire and the invited closing lecture provided him with the opportunity to both highlight his major achievements but provide insights into the direction of the field for the future. The meeting was highly stimulating and successful and the future for the meeting and the research topics covered appears to be very exciting.

Impacts
The meeting effectively disseminated knowledge and insights to all in attendance and sparked numerous informal interactions during the afternoon free times. The meeting was represented by speakers and participants that represented a good mix of young investigators and established investigators and a conscious effort was made to increase the number of women invited speakers and participants overall. In the future increasing the number of participants with an emphasis on increasing the number of women and young investigators in attendance and as invited speakers. A meeting of this sort has a tremendous impact on the direction of the field and the enthusiasm for the research topic.

Publications

  • No publications reported this period